CMPB_SYNP6
ID CMPB_SYNP6 Reviewed; 278 AA.
AC Q5MZ55;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Bicarbonate transport system permease protein CmpB;
GN Name=cmpB; OrderedLocusNames=syc2475_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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 (By similarity). {ECO:0000250}.
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:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; AP008231; BAD80665.1; -; Genomic_DNA.
DR RefSeq; WP_011244785.1; NC_006576.1.
DR AlphaFoldDB; Q5MZ55; -.
DR SMR; Q5MZ55; -.
DR STRING; 269084.syc2475_d; -.
DR EnsemblBacteria; BAD80665; BAD80665; syc2475_d.
DR KEGG; syc:syc2475_d; -.
DR eggNOG; COG0600; Bacteria.
DR OMA; LIEFYRP; -.
DR Proteomes; UP000001175; Chromosome.
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 3: Inferred from homology;
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_0000341961"
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