CSTA_CAMJE
ID CSTA_CAMJE Reviewed; 703 AA.
AC Q0P9Y2;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Peptide transporter CstA {ECO:0000305};
DE AltName: Full=Carbon starvation protein A {ECO:0000303|PubMed:23682166};
GN Name=cstA {ECO:0000303|PubMed:23682166};
GN OrderedLocusNames=Cj0917c {ECO:0000312|EMBL:CAL35037.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=23682166; DOI=10.1099/jmm.0.059345-0;
RA Rasmussen J.J., Vegge C.S., Froekiaer H., Howlett R.M., Krogfelt K.A.,
RA Kelly D.J., Ingmer H.;
RT "Campylobacter jejuni carbon starvation protein A (CstA) is involved in
RT peptide utilization, motility and agglutination, and has a role in
RT stimulation of dendritic cells.";
RL J. Med. Microbiol. 62:1135-1143(2013).
CC -!- FUNCTION: Involved in the uptake of dipeptides and tripeptides. May
CC influence host-pathogen interactions. Involved in motility and
CC agglutination, and has a role in stimulation of dendritic cells.
CC {ECO:0000269|PubMed:23682166}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant has a reduced ability to utilize
CC a number of di- and tri-peptides as nitrogen sources, displays reduced
CC motility and reduced agglutination compared to wild type.
CC {ECO:0000269|PubMed:23682166}.
CC -!- SIMILARITY: Belongs to the peptide transporter carbon starvation (CstA)
CC (TC 2.A.114) family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35037.1; -; Genomic_DNA.
DR PIR; D81365; D81365.
DR RefSeq; WP_002853255.1; NC_002163.1.
DR RefSeq; YP_002344315.1; NC_002163.1.
DR AlphaFoldDB; Q0P9Y2; -.
DR IntAct; Q0P9Y2; 2.
DR STRING; 192222.Cj0917c; -.
DR TCDB; 2.A.114.1.5; the putative peptide transporter carbon starvation csta (csta) family.
DR PaxDb; Q0P9Y2; -.
DR PRIDE; Q0P9Y2; -.
DR EnsemblBacteria; CAL35037; CAL35037; Cj0917c.
DR GeneID; 905216; -.
DR KEGG; cje:Cj0917c; -.
DR PATRIC; fig|192222.6.peg.901; -.
DR eggNOG; COG1966; Bacteria.
DR HOGENOM; CLU_010531_2_0_7; -.
DR OMA; GTISGFH; -.
DR Proteomes; UP000000799; 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:0009267; P:cellular response to starvation; IEA:InterPro.
DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR025299; CstA_C.
DR InterPro; IPR003706; CstA_N.
DR Pfam; PF02554; CstA; 1.
DR Pfam; PF13722; CstA_5TM; 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..703
FT /note="Peptide transporter CstA"
FT /id="PRO_0000443387"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 703 AA; 75792 MW; A171FFCE671E9369 CRC64;
MTQLSTKILW LFVAALGAIC FGYLALQNGE SVSAIYLVVA AVCIYMIGYR FYGSFVAYKV
LELDKNRATP ALVENDGRDF VPTNKAVLFG HHFAAIAGAG PLVGPILAAQ MGYLPSMLWI
LVGGVLAGAV HDFVVLFIST RRKGRSLGEM IKDEMGKFTG GVAMVAIFGI MLIIIAILAM
VVVKALAESP WGLFTIAMTI PIAIFMGIYM RFIRPGRVGE ASIIGFVLLI LAIHYGSVIA
ADPYWAKIFT LEAPTLAIVM MAYGFIASVL PVWFLLAPRD YLSTFLKIGV IVVMAVAIVL
VAPDLQMPKA NTQYFDGTGP VFAGGVFPFL FITIACGAIS GFHALISSGT TPKMLENETH
TLAVGYGSML AESAVAIMAL ICACILHPGL YFAINSSSAL IGTDVVNVAQ TISSWGFSIT
PEEITTLTTN IGEYTILSRT GGAPTFAIGV ALILHELFGG VDLMAFWYHF AILFEALFIL
TAVDAGTRAC RFMVQDILGN VYKPLGDIHN YPAGLLATAL SVAGWGYFLY QGAIDPKGGI
YTLWPLFGVS NQMLAGMALL LATTILVKMG KARYTWVTLV PAVFVLVATL YGGIQKIMPY
EEGNKIANAV SHVAAVSIQS QKIKDLEFKL NNTKDEKEIS TIRKEISIAT QNKVGNLLNA
ILCVFFMIAT LLVIISCIGI CLGKIKIPLK ETKYIKIDEF QKI
