PCXA_SYNJA
ID PCXA_SYNJA Reviewed; 460 AA.
AC Q2JRR7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Proton extrusion protein PcxA {ECO:0000255|HAMAP-Rule:MF_01308};
GN Name=pcxA {ECO:0000255|HAMAP-Rule:MF_01308}; OrderedLocusNames=CYA_2560;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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; CP000239; ABD00679.1; -; Genomic_DNA.
DR RefSeq; WP_011431352.1; NC_007775.1.
DR AlphaFoldDB; Q2JRR7; -.
DR SMR; Q2JRR7; -.
DR STRING; 321327.CYA_2560; -.
DR EnsemblBacteria; ABD00679; ABD00679; CYA_2560.
DR KEGG; cya:CYA_2560; -.
DR eggNOG; ENOG502Z8DN; Bacteria.
DR HOGENOM; CLU_690401_0_0_3; -.
DR OMA; PANRDFI; -.
DR OrthoDB; 1605855at2; -.
DR Proteomes; UP000008818; 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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..460
FT /note="Proton extrusion protein PcxA"
FT /id="PRO_0000293503"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT REGION 84..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 52203 MW; B7D34D4CEAA5844C CRC64;
MGESVLSRLG QWISSTPLRS LDRAYEAALR IKAIEDRYFQ GGSIGSNGNH GQNTSRYFQI
QLRQELRQID LSLAEFRASS VFSRLPDPEQ NGSGPPFSSD KDQAKEAPVG PSENDGKDAE
NGRQSRDPSI LEKLEFIDQV TSRYKRPAAQ PRSTSPPPKS QEQPEPLTSS QPEPSDPSIK
TNLAKTNLDN SNAPVASKTA LLPRSILRTA NQIRRELSSQ AEEELLQEYR SQRTRTLVAV
RFLLLLAILP LLVQIFSKHF LFGPLVDRFQ PREPTILALS YEFQEKALSE FEFFKEKIEF
ERALHHQSPE LDLESEDQLS KKAEELLQKY SRKNLEGLKN VLADVLSLLV FGWLILIGRE
EIEVLKSFLD RLIYGLSDSA KAFIIILFTD VFVGYHSPHG WEVLLSSLAA HLGLPENRNF
IYGFIATFPV FLDTLFKYWI FRYLNRVSPS AVATYHAMND