SAPB_ECOLI
ID SAPB_ECOLI Reviewed; 321 AA.
AC P0AGH3; P76838; Q47623;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putrescine export system permease protein SapB {ECO:0000305};
GN Name=sapB; OrderedLocusNames=b1293, JW1286;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / FRAG5;
RX PubMed=11700350; DOI=10.1099/00221287-147-11-2991;
RA Harms C., Domoto Y., Celik C., Rahe E., Stumpe S., Schmid R., Nakamura T.,
RA Bakker E.P.;
RT "Identification of the ABC protein SapD as the subunit that confers ATP
RT dependence to the K+-uptake systems Trk(H) and Trk(G) from Escherichia coli
RT K-12.";
RL Microbiology 147:2991-3003(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION IN PUTRESCINE EXPORT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=27803167; DOI=10.1074/jbc.m116.762450;
RA Sugiyama Y., Nakamura A., Matsumoto M., Kanbe A., Sakanaka M., Higashi K.,
RA Igarashi K., Katayama T., Suzuki H., Kurihara S.;
RT "A novel putrescine exporter SapBCDF of Escherichia coli.";
RL J. Biol. Chem. 291:26343-26351(2016).
CC -!- FUNCTION: Part of a putrescine export transport system, does not play a
CC role in resistance to antimicrobial peptides.
CC {ECO:0000269|PubMed:27803167}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15919996}.
CC -!- DISRUPTION PHENOTYPE: Single mutation, decreased extracellular
CC putrescine, in an sapBCDF operon deletion no change in resistance to
CC antimicrobial peptide LL-37. Operon deletion has no effect on growth,
CC but if the putrescine importer PuuP is also deleted then growth is
CC slower. {ECO:0000269|PubMed:27803167}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X97282; CAA65938.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74375.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14854.1; -; Genomic_DNA.
DR PIR; H64877; H64877.
DR RefSeq; NP_415809.1; NC_000913.3.
DR RefSeq; WP_000583277.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P0AGH3; -.
DR BioGRID; 4260136; 262.
DR ComplexPortal; CPX-4422; Putative peptide ABC transporter.
DR STRING; 511145.b1293; -.
DR TCDB; 3.A.1.5.42; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AGH3; -.
DR PaxDb; P0AGH3; -.
DR PRIDE; P0AGH3; -.
DR EnsemblBacteria; AAC74375; AAC74375; b1293.
DR EnsemblBacteria; BAA14854; BAA14854; BAA14854.
DR GeneID; 66674880; -.
DR GeneID; 946191; -.
DR KEGG; ecj:JW1286; -.
DR KEGG; eco:b1293; -.
DR PATRIC; fig|1411691.4.peg.986; -.
DR EchoBASE; EB4156; -.
DR eggNOG; COG4168; Bacteria.
DR HOGENOM; CLU_036879_0_3_6; -.
DR InParanoid; P0AGH3; -.
DR OMA; RKEWYAN; -.
DR PhylomeDB; P0AGH3; -.
DR BioCyc; EcoCyc:SAPB-MON; -.
DR BioCyc; MetaCyc:SAPB-MON; -.
DR BRENDA; 7.6.2.11; 2026.
DR PRO; PR:P0AGH3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015489; F:putrescine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015833; P:peptide transport; IC:ComplexPortal.
DR GO; GO:0015847; P:putrescine transport; IMP:EcoCyc.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..321
FT /note="Putrescine export system permease protein SapB"
FT /id="PRO_0000060158"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 30..80
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 102..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 134..174
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 196..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 270..280
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 302..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:27803167"
FT DOMAIN 74..302
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 321 AA; 36038 MW; E50607A4A2C551F2 CRC64;
MIIFTLRRIL LLIVTLFLLT FVGFSLSYFT PHAPLQGASL WNAWVFWFNG LIHWDFGVSS
INGQPIAEQL KEVFPATMEL CILAFGFALI VGIPVGMIAG ITRHKWQDNL INAIALLGFS
IPVFWLALLL TLFCSLTLGW LPVSGRFDLL YEVKPITGFA LIDAWLSDSP WRDEMIMSAI
RHMILPVITL SVAPTTEVIR LMRISTIEVY DQNYVKAAAT RGLSRFTILR RHVLHNALPP
VIPRLGLQFS TMLTLAMITE MVFSWPGLGR WLINAIRQQD YAAISAGVMV CGSLVIIVNV
ISDILGAMAN PLKHKEWYAL R
