ID   PCXA_SYNE7              Reviewed;         421 AA.
AC   Q31PJ8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Proton extrusion protein PcxA {ECO:0000255|HAMAP-Rule:MF_01308};
GN   Name=pcxA {ECO:0000255|HAMAP-Rule:MF_01308};
GN   OrderedLocusNames=Synpcc7942_0991;
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 [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.
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; CP000100; ABB57021.1; -; Genomic_DNA.
DR   RefSeq; WP_011242865.1; NC_007604.1.
DR   AlphaFoldDB; Q31PJ8; -.
DR   SMR; Q31PJ8; -.
DR   STRING; 1140.Synpcc7942_0991; -.
DR   PRIDE; Q31PJ8; -.
DR   EnsemblBacteria; ABB57021; ABB57021; Synpcc7942_0991.
DR   KEGG; syf:Synpcc7942_0991; -.
DR   eggNOG; ENOG502Z8DN; Bacteria.
DR   HOGENOM; CLU_690401_0_0_3; -.
DR   OMA; HSPEGWT; -.
DR   BioCyc; SYNEL:SYNPCC7942_0991-MON; -.
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..421
FT                   /note="Proton extrusion protein PcxA"
FT                   /id="PRO_0000293504"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT   REGION          124..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  48390 MW;  8CA79FAB46D19BDE CRC64;
     MAFFAGISDW VAQRLQRNSE TARLDLERAY EAALYITALE TEYASGRSLR RLPSQLSARQ
     QTSLQAELRQ TLRSLRHYRQ RYRRHQPVQL QAGLALGRPG MGMPTIAHEK LQLIEQVLAR
     YGQPTVHSSN PDDSQLMTSK NNSKPVPDPE SDDEYLISQT SFLPRSIFGA FADLRQQLDP
     KAEDQIVQNF RSRKGKTLIA LRFVLLLVLV PLLTQQISKS FIVGPIVDRL RSQDPEAIFL
     NFQMEEEAFV KLNQYQQLLR FQHYLKEAPP LTEAEIDERV REKAEEIAVE YRQESSNAIK
     NIFADLISAA AFAILLISSQ EEIQLLKSFI DEVVYGISDS AKAFIIILFT DIFVGFHSPH
     GWEVILESIS RHFGIPENRS FIFLFIATFP VILDTIFKYW IFRYLNRISP SAVATYRNMN
     E