SAPC_SHIFL
ID SAPC_SHIFL Reviewed; 296 AA.
AC P0AGH7; Q47624;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Peptide transport system permease protein SapC;
GN Name=sapC; OrderedLocusNames=SF1297, S1379;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42908.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16791.1; -; Genomic_DNA.
DR RefSeq; NP_707201.1; NC_004337.2.
DR RefSeq; WP_001146163.1; NZ_WPGW01000009.1.
DR AlphaFoldDB; P0AGH7; -.
DR SMR; P0AGH7; -.
DR STRING; 198214.SF1297; -.
DR EnsemblBacteria; AAN42908; AAN42908; SF1297.
DR EnsemblBacteria; AAP16791; AAP16791; S1379.
DR GeneID; 1024270; -.
DR GeneID; 66674881; -.
DR KEGG; sfl:SF1297; -.
DR KEGG; sfx:S1379; -.
DR PATRIC; fig|198214.7.peg.1523; -.
DR HOGENOM; CLU_028518_1_1_6; -.
DR OMA; WFAVLPN; -.
DR OrthoDB; 1734230at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 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..296
FT /note="Peptide transport system permease protein SapC"
FT /id="PRO_0000060167"
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; 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
