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CYDD_ECOLI
ID   CYDD_ECOLI              Reviewed;         588 AA.
AC   P29018; P77275; Q47656;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=ATP-binding/permease protein CydD;
GN   Name=cydD; Synonyms=htrD; OrderedLocusNames=b0887, JW0870;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [2]
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   [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 48-588.
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
RC   STRAIN=K12;
RX   PubMed=8380150; DOI=10.1128/jb.175.1.166-175.1993;
RA   Delaney J.M., Wall D., Georgopoulos C.;
RT   "Molecular characterization of the Escherichia coli htrD gene: cloning,
RT   sequence, regulation, and involvement with cytochrome d oxidase.";
RL   J. Bacteriol. 175:166-175(1993).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=1310500; DOI=10.1128/jb.174.4.1240-1247.1992;
RA   Delaney J.M., Ang D., Georgopoulos C.;
RT   "Isolation and characterization of the Escherichia coli htrD gene, whose
RT   product is required for growth at high temperatures.";
RL   J. Bacteriol. 174:1240-1247(1992).
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   -!- MISCELLANEOUS: Required for growth at high temperatures.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Cysteine
CC       exporter (TC 3.A.1.129.1) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA23995.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L21749; AAA66171.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73973.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35612.1; -; Genomic_DNA.
DR   EMBL; L25859; AAC36863.1; -; Unassigned_DNA.
DR   EMBL; M95935; AAA23995.1; ALT_FRAME; Genomic_DNA.
DR   PIR; F64827; F64827.
DR   RefSeq; NP_415407.1; NC_000913.3.
DR   RefSeq; WP_001043598.1; NZ_LN832404.1.
DR   AlphaFoldDB; P29018; -.
DR   SMR; P29018; -.
DR   BioGRID; 4261714; 25.
DR   ComplexPortal; CPX-4601; Glutathione/cysteine ABC exporter complex.
DR   DIP; DIP-9363N; -.
DR   IntAct; P29018; 2.
DR   STRING; 511145.b0887; -.
DR   TCDB; 3.A.1.129.1; the atp-binding cassette (abc) superfamily.
DR   jPOST; P29018; -.
DR   PaxDb; P29018; -.
DR   PRIDE; P29018; -.
DR   EnsemblBacteria; AAC73973; AAC73973; b0887.
DR   EnsemblBacteria; BAA35612; BAA35612; BAA35612.
DR   GeneID; 949052; -.
DR   KEGG; ecj:JW0870; -.
DR   KEGG; eco:b0887; -.
DR   PATRIC; fig|1411691.4.peg.1391; -.
DR   EchoBASE; EB1377; -.
DR   eggNOG; COG4988; Bacteria.
DR   HOGENOM; CLU_000604_84_9_6; -.
DR   InParanoid; P29018; -.
DR   OMA; FPLNWAA; -.
DR   PhylomeDB; P29018; -.
DR   BioCyc; EcoCyc:CYDD-MON; -.
DR   BioCyc; MetaCyc:CYDD-MON; -.
DR   PRO; PR:P29018; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISM:EcoCyc.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR   GO; GO:0005886; C: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; IMP:EcoCyc.
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:0055085; P:transmembrane transport; IBA:GO_Central.
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; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR014216; ABC_transptr_CydD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
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; TIGR02857; CydD; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..588
FT                   /note="ATP-binding/permease protein CydD"
FT                   /id="PRO_0000092244"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        163..183
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        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          24..316
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          350..583
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         383..390
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        64
FT                   /note="Missing (in Ref. 6; AAA23995)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        313
FT                   /note="A -> R (in Ref. 5; AAC36863)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        427
FT                   /note="W -> S (in Ref. 1; AAA66171)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   588 AA;  65056 MW;  8EB3212039E382D0 CRC64;
     MNKSRQKELT RWLKQQSVIS QRWLNISRLL GFVSGILIIA QAWFMARILQ HMIMENIPRE
     ALLLPFTLLV LTFVLRAWVV WLRERVGYHA GQHIRFAIRR QVLDRLQQAG PAWIQGKPAG
     SWATLVLEQI DDMHDYYARY LPQMALAVSV PLLIVVAIFP SNWAAALILL GTAPLIPLFM
     ALVGMGAADA NRRNFLALAR LSGHFLDRLR GMETLRIFGR GEAEIESIRS ASEDFRQRTM
     EVLRLAFLSS GILEFFTSLS IALVAVYFGF SYLGELDFGH YDTGVTLAAG FLALILAPEF
     FQPLRDLGTF YHAKAQAVGA ADSLKTFMET PLAHPQRGEA ELASTDPVTI EAEELFITSP
     EGKTLAGPLN FTLPAGQRAV LVGRSGSGKS SLLNALSGFL SYQGSLRING IELRDLSPES
     WRKHLSWVGQ NPQLPAATLR DNVLLARPDA SEQELQAALD NAWVSEFLPL LPQGVDTPVG
     DQAARLSVGQ AQRVAVARAL LNPCSLLLLD EPAASLDAHS EQRVMEALNA ASLRQTTLMV
     THQLEDLADW DVIWVMQDGR IIEQGRYAEL SVAGGPFATL LAHRQEEI
 
 
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