ID   GSPA_AERHY              Reviewed;         547 AA.
AC   P45754;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=General secretion pathway protein A;
GN   Name=exeA;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RX   PubMed=7961440; DOI=10.1128/jb.176.22.6819-6826.1994;
RA   Jahagirdar R., Howard S.P.;
RT   "Isolation and characterization of a second exe operon required for
RT   extracellular protein secretion in Aeromonas hydrophila.";
RL   J. Bacteriol. 176:6819-6826(1994).
CC   -!- FUNCTION: Involved in a general secretion pathway (GSP) for the export
CC       of proteins.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ExeA family. {ECO:0000305}.
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DR   EMBL; X81473; CAA57225.1; -; Genomic_DNA.
DR   PIR; I39593; I39593.
DR   AlphaFoldDB; P45754; -.
DR   SMR; P45754; -.
DR   STRING; 1448139.AI20_00280; -.
DR   TCDB; 9.B.42.1.1; the exeab (exeab) secretin assembly/export complex.
DR   eggNOG; COG3267; Bacteria.
DR   eggNOG; COG3409; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.101.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   Pfam; PF13401; AAA_22; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47090; SSF47090; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW   Transport.
FT   CHAIN           1..547
FT                   /note="General secretion pathway protein A"
FT                   /id="PRO_0000214993"
FT   REGION          512..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         50..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   547 AA;  60765 MW;  206BD7153AA3F732 CRC64;
     MYTQFFGLSE PPFSISPNPK YLYMSERHGE ALAHLNYGLQ DGGGFVLLTG EVGTGKTTVS
     RCLLQQLPTE TEIAYILNPS LTERDLLAAI CDEFQLPYDK DAGLKLLFDL IRDHLLANLA
     AGKRSVVLVD EAQHLLPGVL EQLRLLTNLE TDEKKLLQVV LIGQPELQQM LRQPLLRQLA
     QRITARYHLL PLSHQDVDAY VRFRLQVAGC VQPIFTPKAL QTLHRLSGGI PRLINLICDR
     ALIAAFARGS HKIVHGDISL AAYEVSGIRD EGTWQSGLMV ALAGALLVAT GWWGWQFFGF
     FPERPVIKVE VPVKVDDTPE QQEQLTRAIN QALEPDSAMQ NLYKVWGYQT ELEEATCDNA
     PRAGLRCQEG DASLAELQAL QHPALISLTD ETGGIYYATL VNLGPDKANL LIGNQSWQVD
     RQWLSDFWGG SYTLLWRMPK GGVALIGNNA GATQVQWLDN ALSRALQQPD RKVRRFDAEL
     KNKLQQFQRE QGLNPDGIAG SNTLLRLNVM AGEPMPKLED ESQRASTPAT PDTMNDEPMV
     TLSEEAS