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CZCO_BACSU
ID   CZCO_BACSU              Reviewed;         345 AA.
AC   O07085; P71024; Q796A5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Uncharacterized oxidoreductase CzcO;
DE            EC=1.-.-.-;
GN   Name=czcO; Synonyms=trkA, yrdP; OrderedLocusNames=BSU26640;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ROLE IN CATION TRANSPORT.
RC   STRAIN=168 / JH642;
RX   PubMed=9099864; DOI=10.1016/s0378-1119(96)00784-6;
RA   Sturr M.G., Ablooglu A.J., Krulwich T.A.;
RT   "A Bacillus subtilis locus encoding several gene products affecting
RT   transport of cations.";
RL   Gene 188:91-94(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9308178; DOI=10.1099/00221287-143-9-2939;
RA   Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J.,
RA   Duesterhoeft A., Ehrlich S.D.;
RT   "Sequence of the Bacillus subtilis genome region in the vicinity of the lev
RT   operon reveals two new extracytoplasmic function RNA polymerase sigma
RT   factors SigV and SigZ.";
RL   Microbiology 143:2939-2943(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   FUNCTION IN CATION AND POTASSIUM TRANSPORT, AND POSSIBLE OXIDOREDUCTASE
RP   ACTIVITY.
RX   PubMed=12100555; DOI=10.1046/j.1365-2958.2002.02998.x;
RA   Guffanti A.A., Wei Y., Rood S.V., Krulwich T.A.;
RT   "An antiport mechanism for a member of the cation diffusion facilitator
RT   family: divalent cations efflux in exchange for K+ and H+.";
RL   Mol. Microbiol. 45:145-153(2002).
CC   -!- FUNCTION: Involved in potassium and divalent cation transport. Enhances
CC       the transport activity of the cation/potassium transporter CzcD.
CC       {ECO:0000269|PubMed:12100555, ECO:0000269|PubMed:9099864}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB53030.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U62055; AAB53030.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U93876; AAB80908.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14605.1; -; Genomic_DNA.
DR   PIR; E69725; E69725.
DR   RefSeq; NP_390541.1; NC_000964.3.
DR   RefSeq; WP_003229874.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O07085; -.
DR   SMR; O07085; -.
DR   STRING; 224308.BSU26640; -.
DR   PaxDb; O07085; -.
DR   PRIDE; O07085; -.
DR   DNASU; 937340; -.
DR   EnsemblBacteria; CAB14605; CAB14605; BSU_26640.
DR   GeneID; 937340; -.
DR   KEGG; bsu:BSU26640; -.
DR   PATRIC; fig|224308.179.peg.2895; -.
DR   eggNOG; COG2072; Bacteria.
DR   InParanoid; O07085; -.
DR   OMA; IFELHTP; -.
DR   PhylomeDB; O07085; -.
DR   BioCyc; BSUB:BSU26640-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   Cadmium; Cell membrane; Cobalt; Cobalt transport; Ion transport; Membrane;
KW   Oxidoreductase; Potassium; Potassium transport; Reference proteome;
KW   Transport; Zinc; Zinc transport.
FT   CHAIN           1..345
FT                   /note="Uncharacterized oxidoreductase CzcO"
FT                   /id="PRO_0000337070"
SQ   SEQUENCE   345 AA;  39065 MW;  D6B2CBFBBD184D19 CRC64;
     MYDTIVIGAG QAGISIGYYL KQSDQKFIIL DKSHEVGESW KDRYDSLVLF TSRMYSSLPG
     MHLEGEKHGF PSKNEIVAYL KKYVKKFEIP IQLRTEVISV LKIKNYFLIK TNREEYQTKN
     LVIATGPFHT PNIPSISKDL SDNINQLHSS QYKNSKQLAY GNVLVVGGGN SGAQIAVELS
     KERVTYLACS NKLVYFPLMI GKRSIFWWFD KLGVLHASHT SIVGKFIQKK GDPVFGHELK
     HAIKQKEIIL KKRVIAAKQN EIIFKDSSTL EVNNIIWATG FRNPLCWINI KGVLDQEGRI
     IHHRGVSPVE GLYFIGLPWQ HKRGSALLQG VGNDAEYIVK QMNGE
 
 
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