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CMPB_SYNE7
ID   CMPB_SYNE7              Reviewed;         278 AA.
AC   Q55106; Q31N50;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Bicarbonate transport system permease protein CmpB;
GN   Name=cmpB; OrderedLocusNames=Synpcc7942_1489;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Omata T.;
RL   Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION IN BICARBONATE TRANSPORT, AND INDUCTION.
RX   PubMed=10557362; DOI=10.1073/pnas.96.23.13571;
RA   Omata T., Price G.D., Badger M.R., Okamura M., Gohta S., Ogawa T.;
RT   "Identification of an ATP-binding cassette transporter involved in
RT   bicarbonate uptake in the cyanobacterium Synechococcus sp. strain PCC
RT   7942.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13571-13576(1999).
RN   [4]
RP   REGULATION BY CMPR.
RX   PubMed=11222586; DOI=10.1128/jb.183.6.1891-1898.2001;
RA   Omata T., Gohta S., Takahashi Y., Harano Y., Maeda S.;
RT   "Involvement of a CbbR homolog in low CO2-induced activation of the
RT   bicarbonate transporter operon in cyanobacteria.";
RL   J. Bacteriol. 183:1891-1898(2001).
CC   -!- FUNCTION: Part of the ABC transporter complex CmpABCD involved in
CC       bicarbonate transport. Probably responsible for the translocation of
CC       the substrate across the membrane (Probable).
CC       {ECO:0000305|PubMed:10557362}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (CmpC and
CC       CmpD), a transmembrane protein (CmpB) and a solute-binding protein
CC       (CmpA). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- INDUCTION: By carbon dioxide-limited conditions, probably via CmpR.
CC       {ECO:0000269|PubMed:10557362}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; D26358; BAA05387.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57519.1; -; Genomic_DNA.
DR   RefSeq; WP_011244785.1; NC_007604.1.
DR   AlphaFoldDB; Q55106; -.
DR   SMR; Q55106; -.
DR   STRING; 1140.Synpcc7942_1489; -.
DR   TCDB; 3.A.1.16.3; the atp-binding cassette (abc) superfamily.
DR   PRIDE; Q55106; -.
DR   EnsemblBacteria; ABB57519; ABB57519; Synpcc7942_1489.
DR   KEGG; syf:Synpcc7942_1489; -.
DR   eggNOG; COG0600; Bacteria.
DR   HOGENOM; CLU_046113_1_1_3; -.
DR   OMA; LIEFYRP; -.
DR   OrthoDB; 1531811at2; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015112; F:nitrate transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR005889; NtrB.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   TIGRFAMs; TIGR01183; ntrB; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Ion transport; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..278
FT                   /note="Bicarbonate transport system permease protein CmpB"
FT                   /id="PRO_0000341960"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          86..267
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   278 AA;  31041 MW;  ED566891FE0002C2 CRC64;
     MVTARETRRN GSRPSGLKKW RQKLDGILLP LAGILGFLII WQIFSSSGAT RLPGPLSLFT
     EERTRELLLY PFLDRGGLDK GLFWQTIASL TRVAQGFSIA AIIGISVGIL VGLNRQLNAM
     LDPLFQFLRM IAPLAWVPIA LVAFQQNQPA AIFVIFITAV WPILINTAEG VRQIPQDYNN
     VARVLRMSKS KYLMKVVLPA ALPYIFTGLR IAIGLSWLAI IAAEIVMSGI VGIGFFIWDA
     YQQNYVSDII LAVIYIGAVG LLLDRFVAWL QRWILRNM
 
 
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