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CZCD_BACSU
ID   CZCD_BACSU              Reviewed;         311 AA.
AC   O07084; P71023; Q796A4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Cadmium, cobalt and zinc/H(+)-K(+) antiporter;
GN   Name=czcD; Synonyms=yrdO; OrderedLocusNames=BSU26650;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-311.
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   [4]
RP   INVOLVEMENT IN RESISTANCE TO COBALT.
RC   STRAIN=BD99 / MS94;
RX   PubMed=10735849; DOI=10.1128/jb.182.8.2088-2095.2000;
RA   Wang W., Guffanti A.A., Wei Y., Ito M., Krulwich T.A.;
RT   "Two types of Bacillus subtilis tetA(L) deletion strains reveal the
RT   physiological importance of TetA(L) in K(+) acquisition as well as in
RT   Na(+), alkali, and tetracycline resistance.";
RL   J. Bacteriol. 182:2088-2095(2000).
RN   [5]
RP   FUNCTION IN DIVALENT CATION EFFLUX.
RC   STRAIN=BD99 / MS94;
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).
RN   [6]
RP   REPRESSION BY CZRA.
RC   STRAIN=168;
RX   PubMed=15948947; DOI=10.1111/j.1365-2958.2005.04642.x;
RA   Moore C.M., Gaballa A., Hui M., Ye R.W., Helmann J.D.;
RT   "Genetic and physiological responses of Bacillus subtilis to metal ion
RT   stress.";
RL   Mol. Microbiol. 57:27-40(2005).
CC   -!- FUNCTION: Involved in divalent cation and potassium homeostasis in the
CC       cell. Catalyzes the active efflux of zinc, cadmium and cobalt, in
CC       exchange for potassium and H(+) ions. {ECO:0000269|PubMed:12100555}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Repressed by CzrA. {ECO:0000269|PubMed:15948947}.
CC   -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC       transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR   EMBL; U93876; AAB80907.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14606.1; -; Genomic_DNA.
DR   EMBL; U62055; AAB53029.1; -; Genomic_DNA.
DR   PIR; C69612; C69612.
DR   RefSeq; NP_390542.1; NC_000964.3.
DR   RefSeq; WP_003229873.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O07084; -.
DR   SMR; O07084; -.
DR   STRING; 224308.BSU26650; -.
DR   TCDB; 2.A.4.1.3; the cation diffusion facilitator (cdf) family.
DR   PaxDb; O07084; -.
DR   PRIDE; O07084; -.
DR   EnsemblBacteria; CAB14606; CAB14606; BSU_26650.
DR   GeneID; 937630; -.
DR   KEGG; bsu:BSU26650; -.
DR   PATRIC; fig|224308.179.peg.2896; -.
DR   eggNOG; COG1230; Bacteria.
DR   InParanoid; O07084; -.
DR   OMA; GHEKMLH; -.
DR   PhylomeDB; O07084; -.
DR   BioCyc; BSUB:BSU26650-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
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:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1510.10; -; 1.
DR   Gene3D; 3.30.70.1350; -; 1.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR027470; Cation_efflux_CTD.
DR   InterPro; IPR036837; Cation_efflux_CTD_sf.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   Pfam; PF16916; ZT_dimer; 1.
DR   SUPFAM; SSF160240; SSF160240; 1.
DR   SUPFAM; SSF161111; SSF161111; 1.
DR   TIGRFAMs; TIGR01297; CDF; 1.
PE   1: Evidence at protein level;
KW   Cadmium; Cell membrane; Cobalt; Cobalt transport; Ion transport; Membrane;
KW   Potassium; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN           1..311
FT                   /note="Cadmium, cobalt and zinc/H(+)-K(+) antiporter"
FT                   /id="PRO_0000337067"
FT   TOPO_DOM        1..12
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..43
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..78
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..157
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        180
FT                   /note="D -> N (in Ref. 3; AAB53029)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   311 AA;  34163 MW;  9F495E9DF8E96DB0 CRC64;
     MGHNHNEGAN KKVLLISFIM ITGYMIIEAI GGFLTNSLAL LSDAGHMLSD SISLMVALIA
     FTLAEKKANH NKTFGYKRFE ILAAVINGAA LILISLYIIY EAIERFSNPP KVATTGMLTI
     SIIGLVVNLL VAWIMMSGGD TKNNLNIRGA YLHVISDMLG SVGAILAAIL IIFFGWGWAD
     PLASIIVAIL VLRSGYNVTK DSIHILMEGT PENIDVSDII RTIEGTEGIQ NIHDLHIWSI
     TSGLNALSCH AVVDDQLTIS ESENILRKIE HELEHKGITH VTIQMETEAH NHDNAILCQP
     KMEKQRDHHH H
 
 
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