ID D2TNE0_CITRI Unreviewed; 310 AA.
AC D2TNE0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=p-hydroxybenzoic acid efflux pump subunit AaeA {ECO:0000256|HAMAP-Rule:MF_01544};
DE Short=pHBA efflux pump protein A {ECO:0000256|HAMAP-Rule:MF_01544};
GN Name=aaeA {ECO:0000256|HAMAP-Rule:MF_01544,
GN ECO:0000313|EMBL:CBG91270.1};
GN OrderedLocusNames=ROD_45741 {ECO:0000313|EMBL:CBG91270.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91270.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG91270.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG91270.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
CC -!- FUNCTION: Forms an efflux pump with AaeB. {ECO:0000256|HAMAP-
CC Rule:MF_01544}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01544}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01544}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477, ECO:0000256|HAMAP-
CC Rule:MF_01544}.
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DR EMBL; FN543502; CBG91270.1; -; Genomic_DNA.
DR RefSeq; WP_012908475.1; NC_013716.1.
DR AlphaFoldDB; D2TNE0; -.
DR STRING; 637910.ROD_45741; -.
DR KEGG; cro:ROD_45741; -.
DR eggNOG; COG1566; Bacteria.
DR HOGENOM; CLU_018816_15_2_6; -.
DR OrthoDB; 9811754at2; -.
DR Proteomes; UP000001889; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR HAMAP; MF_01544; AaeA; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR022871; PHBA_efflux_pump_AaeA.
DR InterPro; IPR006143; RND_pump_MFP.
DR NCBIfam; TIGR01730; RND_mfp; 1.
DR PANTHER; PTHR30367:SF12; P-HYDROXYBENZOIC ACID EFFLUX PUMP SUBUNIT AAEA; 1.
DR PANTHER; PTHR30367; P-HYDROXYBENZOIC ACID EFFLUX PUMP SUBUNIT AAEA-RELATED; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01544};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01544};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01544};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01544};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01544};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01544}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01544"
FT DOMAIN 47..94
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 87..144
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 310 AA; 34787 MW; 4A0CD7EC1F3F0370 CRC64;
MKTLTRKLSR TAITLVLVIL AFIAIFRAWV YYTESPWTRD ARFSADVVAI APDVSGLITH
VEVHDNQLVK KDQVLFTIDQ PRYKKALEEA EADVAYYQVL AQEKRQEASR RNRLGVQAMS
REEIDQANNV LQTVLHQLAK AQATRDLAKL DLERTVIRAP ADGWVTNLNV YTGEFITRGS
TAVALVKKNS FYVLAYMEET KLEGVRPGYR AEITPLGSNT VLKGTVDSVA AGVTNASSTR
DDKGMATIDS NLEWVRLAQR VPVRIRLDSQ QENLWPAGTT ATVVVTGERD RDASNDSFFR
KMAHRLREFG
//
