SAPC_ECOLI
ID SAPC_ECOLI Reviewed; 296 AA.
AC P0AGH5; Q47624;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putrescine export system permease protein SapC {ECO:0000305};
GN Name=sapC; OrderedLocusNames=b1292, JW1285;
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. {ECO:0000269|PubMed:27803167}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000305}.
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DR EMBL; X97282; CAA65939.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74374.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14845.1; -; Genomic_DNA.
DR PIR; G64877; G64877.
DR RefSeq; NP_415808.1; NC_000913.3.
DR RefSeq; WP_001146163.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P0AGH5; -.
DR SMR; P0AGH5; -.
DR BioGRID; 4263003; 195.
DR ComplexPortal; CPX-4422; Putative peptide ABC transporter.
DR DIP; DIP-10824N; -.
DR IntAct; P0AGH5; 1.
DR STRING; 511145.b1292; -.
DR TCDB; 3.A.1.5.42; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AGH5; -.
DR PaxDb; P0AGH5; -.
DR PRIDE; P0AGH5; -.
DR EnsemblBacteria; AAC74374; AAC74374; b1292.
DR EnsemblBacteria; BAA14845; BAA14845; BAA14845.
DR GeneID; 66674881; -.
DR GeneID; 945266; -.
DR KEGG; ecj:JW1285; -.
DR KEGG; eco:b1292; -.
DR PATRIC; fig|1411691.4.peg.987; -.
DR EchoBASE; EB4157; -.
DR eggNOG; COG4171; Bacteria.
DR HOGENOM; CLU_028518_1_1_6; -.
DR InParanoid; P0AGH5; -.
DR OMA; WFAVLPN; -.
DR PhylomeDB; P0AGH5; -.
DR BioCyc; EcoCyc:SAPC-MON; -.
DR BioCyc; MetaCyc:SAPC-MON; -.
DR BRENDA; 7.6.2.11; 2026.
DR PRO; PR:P0AGH5; -.
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: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 InterPro; IPR025966; OppC_N.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF12911; OppC_N; 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..296
FT /note="Putrescine export system permease protein SapC"
FT /id="PRO_0000060163"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 50..98
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 120..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 155..196
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 218..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 244..257
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 279..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:27803167"
FT DOMAIN 99..284
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 296 AA; 31548 MW; 57CD1F8180BF0B7C CRC64;
MPYDSVYSEK RPPGTLRTAW RKFYSDASAM VGLYGCAGLA VLCIFGGWFA PYGIDQQFLG
YQLLPPSWSR YGEVSFFLGT DDLGRDVLSR LLSGAAPTVG GAFVVTLAAT ICGLVLGTFA
GATHGLRSAV LNHILDTLLA IPSLLLAIIV VAFAGPSLSH AMFAVWLALL PRMVRSIYSM
VHDELEKEYV IAARLDGAST LNILWFAVMP NITAGLVTEI TRALSMAILD IAALGFLDLG
AQLPSPEWGA MLGDALELIY VAPWTVMLPG AAIMISVLLV NLLGDGVRRA IIAGVE
