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SAPB_ECO57
ID   SAPB_ECO57              Reviewed;         321 AA.
AC   P0AGH4; P76838; Q47623;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Peptide transport system permease protein SapB;
GN   Name=sapB; OrderedLocusNames=Z2496, ECs1870;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Involved in a peptide intake transport system that plays a
CC       role in the resistance to antimicrobial peptides. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. OppBC subfamily. {ECO:0000305}.
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DR   EMBL; AE005174; AAG56511.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35293.1; -; Genomic_DNA.
DR   PIR; C85756; C85756.
DR   PIR; F90862; F90862.
DR   RefSeq; NP_309897.1; NC_002695.1.
DR   RefSeq; WP_000583277.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AGH4; -.
DR   STRING; 155864.EDL933_2391; -.
DR   EnsemblBacteria; AAG56511; AAG56511; Z2496.
DR   EnsemblBacteria; BAB35293; BAB35293; ECs_1870.
DR   GeneID; 66674880; -.
DR   GeneID; 912731; -.
DR   KEGG; ece:Z2496; -.
DR   KEGG; ecs:ECs_1870; -.
DR   PATRIC; fig|386585.9.peg.1972; -.
DR   eggNOG; COG4168; Bacteria.
DR   HOGENOM; CLU_036879_0_3_6; -.
DR   OMA; RKEWYAN; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..321
FT                   /note="Peptide transport system permease protein SapB"
FT                   /id="PRO_0000060159"
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"
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
 
 
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