PCXA_SYNJB
ID PCXA_SYNJB Reviewed; 460 AA.
AC Q2JN84;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Proton extrusion protein PcxA {ECO:0000255|HAMAP-Rule:MF_01308};
GN Name=pcxA {ECO:0000255|HAMAP-Rule:MF_01308}; OrderedLocusNames=CYB_0810;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
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; CP000240; ABD01791.1; -; Genomic_DNA.
DR RefSeq; WP_011432448.1; NC_007776.1.
DR AlphaFoldDB; Q2JN84; -.
DR STRING; 321332.CYB_0810; -.
DR KEGG; cyb:CYB_0810; -.
DR eggNOG; ENOG502Z8DN; Bacteria.
DR HOGENOM; CLU_690401_0_0_3; -.
DR OMA; PANRDFI; -.
DR OrthoDB; 1605855at2; -.
DR Proteomes; UP000001938; 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..460
FT /note="Proton extrusion protein PcxA"
FT /id="PRO_0000293502"
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 82..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 52064 MW; 00B9C90435EC1C4D CRC64;
MGESVLSRLG QWISNTPLRS LDQAYEAALR IKAIEDQYFQ GGSIGSNGQH GQNVSRYFQI
QLRRQLRQID LRLAEFRASS AFSRLPDPEQ NGSGPTSAQD KAQQLHAAEA NVSESSSENS
ENGRQRRDLS ILEKLQFIDQ VTSRYKRPTR KSQPISASIS TSPEPLERPE QPTSTQPSSS
NVSVKAGSGN GAAPVASKAA ILPRSILRTA SQIRRELSSQ AEEELIQEYR EARTRTLVSI
RFLLLLAILP LLTQILSKNF LFGPLVDHLQ QREPAIVALS HEFQEKALTE FEFFKERMEF
ERALHHQSPE WDLESADQLS MKAEELLKKY SRRNSEGLKN ILADLLSLLV FGWLIFVGRE
EIEVLKSFLD RLIYGLSDSA KAFIIILFTD VFVGYHSPHG WEVLLGNLAA HLGVPENRDF
IYGFIATFPV FLDTLFKYWI FRYLNRVSPS SVATYRAMND