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Database: UniProt
Entry: A0A924CQE1_9CYAN
LinkDB: A0A924CQE1_9CYAN
Original site: A0A924CQE1_9CYAN 
ID   A0A924CQE1_9CYAN        Unreviewed;       457 AA.
AC   A0A924CQE1;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   18-JUN-2025, entry version 10.
DE   RecName: Full=Proton extrusion protein PxcA {ECO:0000256|HAMAP-Rule:MF_01308};
GN   Name=pxcA {ECO:0000256|HAMAP-Rule:MF_01308};
GN   ORFNames=H7237_07420 {ECO:0000313|EMBL:MBC7516241.1};
OS   Leptolyngbyaceae cyanobacterium LF-bin-369.
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC   Leptolyngbyaceae.
OX   NCBI_TaxID=2804781 {ECO:0000313|EMBL:MBC7516241.1, ECO:0000313|Proteomes:UP000635701};
RN   [1] {ECO:0000313|EMBL:MBC7516241.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LF-bin-369 {ECO:0000313|EMBL:MBC7516241.1};
RA   Zeng Y.;
RT   "Metagenome-assembled genomes from the Lille Firn glacier at the Villum
RT   Research Station in northeast Greenland.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for H(+) efflux immediately after light irradiation
CC       to form a rapid H(+) concentration gradient across the thylakoid
CC       membranes. Together with PxcL, contributes to transient H(+) uptake
CC       following dark to light transition. {ECO:0000256|HAMAP-Rule:MF_01308}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01308}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01308}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CemA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01308}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBC7516241.1}.
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DR   EMBL; JACMPV010000245; MBC7516241.1; -; Genomic_DNA.
DR   Proteomes; UP000635701; Unassembled WGS sequence.
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_PxcA; 1.
DR   InterPro; IPR004282; CemA.
DR   PANTHER; PTHR33650:SF2; CHLOROPLAST ENVELOPE MEMBRANE PROTEIN; 1.
DR   PANTHER; PTHR33650; CHLOROPLAST ENVELOPE MEMBRANE PROTEIN-RELATED; 1.
DR   Pfam; PF03040; CemA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01308};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01308};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01308};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01308};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01308};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01308};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01308};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01308}.
FT   TRANSMEM        225..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01308"
FT   TRANSMEM        416..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01308"
SQ   SEQUENCE   457 AA;  52023 MW;  7993DBDD967A0A65 CRC64;
     MKTSFWSKVT GYVRHAENWY LTTPDRALDE AYDAALMIQA IENEHFKGLK ILPQNSNNLG
     QEAFIYFDQE REKHLKLLKL RLSEFRLSRS TVDATNPKES RLRSDRALTD DRSTAILEKL
     KFIDQVIARY PSQALALVQS TAVQTVPKTL TSYTPKDAER RSDFEVANRK PAATKLGSLE
     SITDKTGVLP RSILGTINRL KRDLNPAGEV EAIQDFQTKR MRTKIAIRFM LILVAVPLLM
     QISIRNFALS DRLIPGHLIS QRFAVVNPAS IFINGEMSEE ALKELSQFEE KIKFENILKE
     AIGQELVTPE IREEKIRDKV DEIAKDYSRR SSSAVKNWIS DLAGVVAFVF ILTKGKAEMQ
     ILKDFIDEVS YGLSDSAKAF IIILFTDIFV GFHSPHGWEV LLEGVAQHFG LAANRSYISL
     FIATFPVILD TIFKYWIFRY LNRISPSAVA TYKDMNE
//
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