SAPC_SALTY
ID SAPC_SALTY Reviewed; 296 AA.
AC P0A2J5; P36669;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Peptide transport system permease protein SapC;
GN Name=sapC {ECO:0000303|PubMed:8223423}; OrderedLocusNames=STM1694;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, OPERON STRUCTURE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=8223423; DOI=10.1002/j.1460-2075.1993.tb06089.x;
RA Parra-Lopez C., Baer M.T., Groisman E.A.;
RT "Molecular genetic analysis of a locus required for resistance to
RT antimicrobial peptides in Salmonella typhimurium.";
RL EMBO J. 12:4053-4062(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Involved in a peptide intake transport system that plays a
CC role in the resistance to antimicrobial peptides.
CC {ECO:0000269|PubMed:8223423}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Part of the sapA-sapB-sapC-sapD-sapF operon, RNA detected in
CC mid-log phase cells. {ECO:0000269|PubMed:8223423}.
CC -!- DISRUPTION PHENOTYPE: Loss of resistance to protamine.
CC {ECO:0000269|PubMed:8223423}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000305}.
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DR EMBL; X74212; CAA52286.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20611.1; -; Genomic_DNA.
DR PIR; S39587; S39587.
DR RefSeq; NP_460652.1; NC_003197.2.
DR RefSeq; WP_001146150.1; NC_003197.2.
DR AlphaFoldDB; P0A2J5; -.
DR SMR; P0A2J5; -.
DR STRING; 99287.STM1694; -.
DR TCDB; 3.A.1.5.5; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0A2J5; -.
DR EnsemblBacteria; AAL20611; AAL20611; STM1694.
DR GeneID; 1253212; -.
DR KEGG; stm:STM1694; -.
DR PATRIC; fig|99287.12.peg.1788; -.
DR HOGENOM; CLU_028518_1_1_6; -.
DR OMA; WFAVLPN; -.
DR PhylomeDB; P0A2J5; -.
DR BioCyc; SENT99287:STM1694-MON; -.
DR Proteomes; UP000001014; 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 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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..296
FT /note="Peptide transport system permease protein SapC"
FT /id="PRO_0000060166"
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"
FT DOMAIN 99..284
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 296 AA; 31548 MW; 4231DF9F4C1A19B4 CRC64;
MPYDSVYSEK RPPGTLRTAW RKFYSDAPAM VGLYGCAGLA LLCIFGGWIA PYGIDQQFLG
YQLLPPSWSR YGEVSFFLGT DDLGRDVLSR LLSGAAPTVG GAFIVTLAAT LCGLVLGVVA
GATHGLRSAV LNHILDTLLS IPSLLLAIIV VAFAGPHLSH AMFAVWLALL PRMVRSVYSM
VHDELEKEYV IAARLDGATT LNILWFAILP NITAGLVTEI TRALSMAILD IAALGFLDLG
AQLPSPEWGA MLGDALELIY VAPWTVMLPG AAITLSVLLV NLLGDGIRRA IIAGVE
