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PCXA_ACAM1
ID   PCXA_ACAM1              Reviewed;         482 AA.
AC   B0CG09;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Proton extrusion protein PcxA {ECO:0000255|HAMAP-Rule:MF_01308};
GN   Name=pcxA {ECO:0000255|HAMAP-Rule:MF_01308}; OrderedLocusNames=AM1_4479;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017;
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC   -!- FUNCTION: Involved in light-induced Na(+)-dependent proton extrusion.
CC       Also seems to be involved in CO(2) transport. {ECO:0000255|HAMAP-
CC       Rule:MF_01308}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01308}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01308}.
CC   -!- SIMILARITY: Belongs to the Cema family. {ECO:0000305}.
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DR   EMBL; CP000828; ABW29456.1; -; Genomic_DNA.
DR   RefSeq; WP_012164771.1; NC_009925.1.
DR   AlphaFoldDB; B0CG09; -.
DR   STRING; 329726.AM1_4479; -.
DR   PRIDE; B0CG09; -.
DR   EnsemblBacteria; ABW29456; ABW29456; AM1_4479.
DR   KEGG; amr:AM1_4479; -.
DR   eggNOG; ENOG502Z8DN; Bacteria.
DR   HOGENOM; CLU_690401_0_0_3; -.
DR   OMA; PANRDFI; -.
DR   OrthoDB; 1605855at2; -.
DR   Proteomes; UP000000268; 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:0015078; F:proton transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01308; CemA; 1.
DR   InterPro; IPR004282; CemA.
DR   PANTHER; PTHR33650; PTHR33650; 1.
DR   Pfam; PF03040; CemA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..482
FT                   /note="Proton extrusion protein PcxA"
FT                   /id="PRO_0000346536"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
SQ   SEQUENCE   482 AA;  54781 MW;  DCED882D119BBBDA CRC64;
     MSSSSPNPFR RSLKFVEQWY RETPQRALDG AYEAARAIEE IEKKHFKGQP VPLRIRTESV
     MTNYFQSEVQ KNLQFIQTRL REFKSSSLVV EVADKLKPPS IPPAPTPLDT PNTIDFTDEY
     DVTSEEYSSE LVSPSIDAQG SLDKLAFIDA VLKRYRSASI QREAAAAASK AARASAPKSG
     SEMKKNIPQP LPIQSAQNSL YESEFISDDI TEDPSKLDSS SFIPRSILRT ATRFRKELNP
     DPGTEDDILN DFRNSRVRTR AAVSFVLGLM IVPLLTQQVS KNLVIGPFVD KLKGPEQIEI
     RINPEIENEV LTELARFEER LKFESLTSPI PLSPAEIQFQ LKAKAEDLKE EYQWDLRQPL
     KNAISDLFSL VALAIYFVLN RQKIAVLKSF FDEIIYGLSD SAKAFIIILF TDVFVGFHSP
     HGWEVIVESV LSHFGLPQDR NFINMFIATF PVMLDTVFKY WIFRYLNQIS PSAVATYRNM
     NE
 
 
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