CSTA_ECOLI
ID CSTA_ECOLI Reviewed; 701 AA.
AC P15078; P23517; P77740;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Peptide transporter CstA {ECO:0000305};
DE AltName: Full=Carbon starvation protein A {ECO:0000305};
GN Name=cstA {ECO:0000303|PubMed:1848300}; Synonyms=ybdC;
GN OrderedLocusNames=b0598, JW0590;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1848300; DOI=10.1016/0022-2836(91)90879-b;
RA Schultz J.E., Matin A.;
RT "Molecular and functional characterization of a carbon starvation gene of
RT Escherichia coli.";
RL J. Mol. Biol. 218:129-140(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200.
RX PubMed=2521622; DOI=10.1128/jb.171.2.791-798.1989;
RA Liu J., Duncan K., Walsh C.T.;
RT "Nucleotide sequence of a cluster of Escherichia coli enterobactin
RT biosynthesis genes: identification of entA and purification of its product
RT 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase.";
RL J. Bacteriol. 171:791-798(1989).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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 [7]
RP TRANSLATION REGULATION.
RX PubMed=12867454; DOI=10.1128/jb.185.15.4450-4460.2003;
RA Dubey A.K., Baker C.S., Suzuki K., Jones A.D., Pandit P., Romeo T.,
RA Babitzke P.;
RT "CsrA regulates translation of the Escherichia coli carbon starvation gene,
RT cstA, by blocking ribosome access to the cstA transcript.";
RL J. Bacteriol. 185:4450-4460(2003).
CC -!- FUNCTION: Involved in peptide utilization during carbon starvation.
CC {ECO:0000269|PubMed:1848300}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by carbon starvation. Induction requires the cAMP-
CC cAMP receptor protein (CRP) complex (PubMed:1848300). The carbon
CC storage regulator CsrA regulates translation of cstA by sterically
CC interfering with ribosome binding (PubMed:12867454).
CC {ECO:0000269|PubMed:12867454, ECO:0000269|PubMed:1848300}.
CC -!- SIMILARITY: Belongs to the peptide transporter carbon starvation (CstA)
CC (TC 2.A.114) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37087.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X52904; CAA37086.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X52904; CAA37087.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U82598; AAB40798.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73699.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35227.1; -; Genomic_DNA.
DR EMBL; M24148; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR PIR; D64793; Q0ECNA.
DR RefSeq; NP_415130.1; NC_000913.3.
DR RefSeq; WP_001043156.1; NZ_SSZK01000032.1.
DR AlphaFoldDB; P15078; -.
DR BioGRID; 4260985; 5.
DR STRING; 511145.b0598; -.
DR TCDB; 2.A.114.1.1; the putative peptide transporter carbon starvation csta (csta) family.
DR jPOST; P15078; -.
DR PaxDb; P15078; -.
DR PRIDE; P15078; -.
DR EnsemblBacteria; AAC73699; AAC73699; b0598.
DR EnsemblBacteria; BAA35227; BAA35227; BAA35227.
DR GeneID; 945213; -.
DR KEGG; ecj:JW0590; -.
DR KEGG; eco:b0598; -.
DR PATRIC; fig|1411691.4.peg.1671; -.
DR EchoBASE; EB0165; -.
DR eggNOG; COG1966; Bacteria.
DR InParanoid; P15078; -.
DR OMA; MLAESFV; -.
DR PhylomeDB; P15078; -.
DR BioCyc; EcoCyc:EG10167-MON; -.
DR BioCyc; MetaCyc:EG10167-MON; -.
DR PRO; PR:P15078; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005477; F:pyruvate secondary active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0031669; P:cellular response to nutrient levels; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEP:EcoCyc.
DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR GO; GO:0006849; P:plasma membrane pyruvate transport; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..701
FT /note="Peptide transporter CstA"
FT /id="PRO_0000190046"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..33
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..117
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..189
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..255
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..324
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..395
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..463
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..550
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..643
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 129
FT /note="A -> G (in Ref. 1; CAA37086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 75105 MW; 2DA85B2D96FD19E5 CRC64;
MNKSGKYLVW TVLSVMGAFA LGYIALNRGE QINALWIVVA SVCIYLIAYR FYGLYIAKNV
LAVDPTRMTP AVRHNDGLDY VPTDKKVLFG HHFAAIAGAG PLVGPVLAAQ MGYLPGMIWL
LAGVVLAGAV QDFMVLFVST RRDGRSLGEL VKEEMGPTAG VIALVACFMI MVIILAVLAM
IVVKALTHSP WGTYTVAFTI PLALFMGIYL RYLRPGRIGE VSVIGLVFLI FAIISGGWVA
ESPTWAPYFD FTGVQLTWML VGYGFVAAVL PVWLLLAPRD YLSTFLKIGT IVGLAVGILI
MRPTLTMPAL TKFVDGTGPV WTGNLFPFLF ITIACGAVSG FHALISSGTT PKMLANEGQA
CFIGYGGMLM ESFVAIMALV SACIIDPGVY FAMNSPMAVL APAGTADVVA SAAQVVSSWG
FSITPDTLNQ IASEVGEQSI ISRAGGAPTL AVGMAYILHG ALGGMMDVAF WYHFAILFEA
LFILTAVDAG TRAARFMLQD LLGVVSPGLK RTDSLPANLL ATALCVLAWG YFLHQGVVDP
LGGINTLWPL FGIANQMLAG MALMLCAVVL FKMKRQRYAW VALVPTAWLL ICTLTAGWQK
AFSPDAKVGF LAIANKFQAM IDSGNIPSQY TESQLAQLVF NNRLDAGLTI FFMVVVVVLA
LFSIKTALAA LKDPKPTAKE TPYEPMPENV EEIVAQAKGA H
