Escherichia coli K-12 substr. MG1655 Polypeptide: ATP binding protein SapF of predicted ABC transporter

Gene: sapF Accession Numbers: EG12305 (EcoCyc), b1290, ECK1285

Regulation Summary Diagram: ?

Regulation summary diagram for sapF

Component of: putative ABC transporter SapABCDF (extended summary available)

Locations: cytosol, inner membrane

Map Position: [1,349,852 <- 1,350,658] (29.09 centisomes, 105°)
Length: 807 bp / 268 aa

Molecular Weight of Polypeptide: 30.57 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0004339 , DIP:DIP-35903N , EchoBASE:EB2211 , EcoGene:EG12305 , EcoliWiki:b1290 , ModBase:P0AAH8 , OU-Microarray:b1290 , PortEco:sapF , PR:PRO_000023908 , Protein Model Portal:P0AAH8 , RefSeq:NP_415806 , RegulonDB:EG12305 , SMR:P0AAH8 , String:511145.b1290 , UniProt:P0AAH8

Relationship Links: InterPro:IN-FAMILY:IPR003439 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR017871 , InterPro:IN-FAMILY:IPR027417 , Pfam:IN-FAMILY:PF00005 , Prosite:IN-FAMILY:PS00211 , Prosite:IN-FAMILY:PS50893 , Smart:IN-FAMILY:SM00382

In Paralogous Gene Group: 23 (75 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a, Linton98]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0015833 - peptide transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA01a, Linton98]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0055052 - ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing Inferred by computational analysis [Linton98]

MultiFun Terms: metabolism carbon utilization amino acids
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily ATP binding cytoplasmic component

Essentiality data for sapF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of: putative ABC transporter SapABCDF

Subunit composition of putative ABC transporter SapABCDF = [SapF][SapD][SapB][SapC][SapA]
         ATP binding protein SapF of predicted ABC transporter = SapF
         ATP binding protein implicated in Trk mediated K+ uptake = SapD (summary available)
         integral membrane protein SapB of predicted ABC transporter = SapB
         integral membrane protein SapC of predicted ABC transporter = SapC
         periplasmic binding protein SapA of predicted ABC transporter = SapA

In Salmonella typhimurium the multicistronic operon sapABCDF is required for virulence and resistance to the antimicrobial peptides melittin and protamine. Based on sequence similarity and hydrophobicity analysis, SapA is a putative periplasmic binding protein, SapB and SapC are both transmembrane proteins and SapD and SapF are the ATP-binding proteins of the complex. Thus in S. typhimurium the Sap system may mediate resistance to antimicrobial peptides by transporting them into the cytoplasm where they can be further degraded [ParraLopez93].

The Sap proteins of E. coli K-12 are highly identical to those from S. typhimurium (95-98% at the amino acid level), however their function is not fully understood and their role in resistance to antimicrobial peptides has been questioned [Stumpe, Harms01]. SapD (also known as TrkE) has been implicated in conferring ATP dependence to the K+ uptake proteins TrkG and TrkH which are not related to the ABC superfamily [Dosch91, Harms01]. Mutation experiments suggest that ATP binding to SapD rather than ATP hydrolysis is sufficient for restoring TrkH mediated K+ uptake in E. coli [Harms01].

sap: sensitive to antimicrobial peptides

Locations: inner membrane

GO Terms:

Cellular Component: GO:0055052 - ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing Inferred by computational analysis [Linton98]

Last-Curated ? 11-Feb-2014 by Mackie A , Macquarie University

Sequence Features

Protein sequence of ATP binding protein SapF of predicted ABC transporter with features indicated

Feature Class Location Citations Comment
Conserved-Region 6 -> 251
UniProt: ABC transporter;
Nucleotide-Phosphate-Binding-Region 47 -> 54
UniProt: ATP; Non-Experimental Qualifier: potential;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b1290 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12305; confirmed by SwissProt match.


Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Dosch91: Dosch DC, Helmer GL, Sutton SH, Salvacion FF, Epstein W (1991). "Genetic analysis of potassium transport loci in Escherichia coli: evidence for three constitutive systems mediating uptake potassium." J Bacteriol 1991;173(2);687-96. PMID: 1987159

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Harms01: Harms C, Domoto Y, Celik C, Rahe E, Stumpe S, Schmid R, Nakamura T, Bakker EP (2001). "Identification of the ABC protein SapD as the subunit that confers ATP dependence to the K+-uptake systems Trk(H) and Trk(G) from Escherichia coli K-12." Microbiology 2001;147(Pt 11);2991-3003. PMID: 11700350

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Linton98: Linton KJ, Higgins CF (1998). "The Escherichia coli ATP-binding cassette (ABC) proteins." Mol Microbiol 1998;28(1);5-13. PMID: 9593292

ParraLopez93: Parra-Lopez C, Baer MT, Groisman EA (1993). "Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium." EMBO J 1993;12(11);4053-62. PMID: 8223423

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Stumpe: Stumpe S, Bakker EP "Requirement of a large K+-uptake capacity and of extracytoplasmic protease activity for protamine resistance of Escherichia coli." Arch Microbiol 167(2-3);126-36. PMID: 9133319

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Oct 9, 2015, biocyc13.