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CYDC_ECOLI
ID   CYDC_ECOLI              Reviewed;         573 AA.
AC   P23886;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   03-AUG-2022, entry version 179.
DE   RecName: Full=ATP-binding/permease protein CydC;
GN   Name=cydC; Synonyms=mdrA, mdrH, surB; OrderedLocusNames=b0886, JW0869;
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 / MC1061 / ATCC 53338 / DSM 7140;
RX   PubMed=8331068; DOI=10.1128/jb.175.14.4364-4374.1993;
RA   Shrader T.E., Tobias J.W., Varshavsky A.;
RT   "The N-end rule in Escherichia coli: cloning and analysis of the leucyl,
RT   phenylalanyl-tRNA-protein transferase gene aat.";
RL   J. Bacteriol. 175:4364-4374(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8276245; DOI=10.1101/gad.7.12b.2629;
RA   Siegele D.D., Kolter R.;
RT   "Isolation and characterization of an Escherichia coli mutant defective in
RT   resuming growth after starvation.";
RL   Genes Dev. 7:2629-2640(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-453.
RX   PubMed=7934832; DOI=10.1111/j.1365-2958.1993.tb02673.x;
RA   Poole R.K., Hatch L., Cleeter M.W.J., Gibson F., Cox G.B., Wu G.;
RT   "Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC
RT   and cydD genes suggest that they encode the components of an ABC membrane
RT   transporter.";
RL   Mol. Microbiol. 10:421-430(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 449-504.
RX   PubMed=1909328; DOI=10.1016/s0021-9258(18)55327-8;
RA   Cummings H.S., Sands J.F., Foreman P.C., Fraser J., Hershey J.W.B.;
RT   "Structure and expression of the infA operon encoding translational
RT   initiation factor IF1. Transcriptional control by growth rate.";
RL   J. Biol. Chem. 266:16491-16498(1991).
RN   [8]
RP   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).
CC   -!- FUNCTION: Somehow involved in the cytochrome D branch of aerobic
CC       respiration. Seems to be a component of a transport system.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15919996}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Cysteine
CC       exporter (TC 3.A.1.129.1) family. {ECO:0000305}.
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DR   EMBL; L10383; AAA03230.1; -; Unassigned_DNA.
DR   EMBL; L25859; AAC36864.1; -; Unassigned_DNA.
DR   EMBL; U00096; AAC73972.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35611.1; -; Genomic_DNA.
DR   EMBL; M63145; AAC36909.1; -; Genomic_DNA.
DR   EMBL; L21749; AAA66172.1; -; Genomic_DNA.
DR   PIR; B36888; B36888.
DR   RefSeq; NP_415406.1; NC_000913.3.
DR   RefSeq; WP_001202177.1; NZ_LN832404.1.
DR   AlphaFoldDB; P23886; -.
DR   SMR; P23886; -.
DR   BioGRID; 4260004; 302.
DR   ComplexPortal; CPX-4601; Glutathione/cysteine ABC exporter complex.
DR   DIP; DIP-9362N; -.
DR   IntAct; P23886; 6.
DR   STRING; 511145.b0886; -.
DR   TCDB; 3.A.1.129.1; the atp-binding cassette (abc) superfamily.
DR   jPOST; P23886; -.
DR   PaxDb; P23886; -.
DR   PRIDE; P23886; -.
DR   EnsemblBacteria; AAC73972; AAC73972; b0886.
DR   EnsemblBacteria; BAA35611; BAA35611; BAA35611.
DR   GeneID; 945504; -.
DR   KEGG; ecj:JW0869; -.
DR   KEGG; eco:b0886; -.
DR   PATRIC; fig|1411691.4.peg.1392; -.
DR   EchoBASE; EB0012; -.
DR   eggNOG; COG4987; Bacteria.
DR   HOGENOM; CLU_000604_84_9_6; -.
DR   InParanoid; P23886; -.
DR   OMA; VYQEIYY; -.
DR   PhylomeDB; P23886; -.
DR   BioCyc; EcoCyc:CYDC-MON; -.
DR   BioCyc; MetaCyc:CYDC-MON; -.
DR   PRO; PR:P23886; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISM:EcoCyc.
DR   GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:EcoCyc.
DR   GO; GO:0045454; P:cell redox homeostasis; IC:ComplexPortal.
DR   GO; GO:0033228; P:cysteine export across plasma membrane; IDA:EcoCyc.
DR   GO; GO:0034775; P:glutathione transmembrane transport; IDA:EcoCyc.
DR   GO; GO:0070453; P:regulation of heme biosynthetic process; IMP:EcoCyc.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR014223; ABC_CydC.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   TIGRFAMs; TIGR02868; CydC; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..573
FT                   /note="ATP-binding/permease protein CydC"
FT                   /id="PRO_0000092241"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          18..306
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          339..572
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         373..380
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        289
FT                   /note="A -> R (in Ref. 2; AAC36864)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        480..481
FT                   /note="LR -> PG (in Ref. 2; AAC36864)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504
FT                   /note="G -> A (in Ref. 7; AAC36909)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   573 AA;  62920 MW;  ACF4E7087EEEADAD CRC64;
     MRALLPYLAL YKRHKWMLSL GIVLAIVTLL ASIGLLTLSG WFLSASAVAG VAGLYSFNYM
     LPAAGVRGAA ITRTAGRYFE RLVSHDATFR VLQHLRIYTF SKLLPLSPAG LARYRQGELL
     NRVVADVDTL DHLYLRVISP LVGAFVVIMV VTIGLSFLDF TLAFTLGGIM LLTLFLMPPL
     FYRAGKSTGQ NLTHLRGQYR QQLTAWLQGQ AELTIFGASD RYRTQLENTE IQWLEAQRRQ
     SELTALSQAI MLLIGALAVI LMLWMASGGV GGNAQPGALI ALFVFCALAA FEALAPVTGA
     FQHLGQVIAS AVRISDLTDQ KPEVTFPDTQ TRVADRVSLT LRDVQFTYPE QSQQALKGIS
     LQVNAGEHIA ILGRTGCGKS TLLQQLTRAW DPQQGEILLN DSPIASLNEA ALRQTISVVP
     QRVHLFSATL RDNLLLASPG SSDEALSEIL RRVGLEKLLE DAGLNSWLGE GGRQLSGGEL
     RRLAIARALL HDAPLVLLDE PTEGLDATTE SQILELLAEM MREKTVLMVT HRLRGLSRFQ
     QIIVMDNGQI IEQGTHAELL ARQGRYYQFK QGL
 
 
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