AAEB_SALTY
ID AAEB_SALTY Reviewed; 655 AA.
AC Q8ZLP5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=p-hydroxybenzoic acid efflux pump subunit AaeB {ECO:0000255|HAMAP-Rule:MF_01545};
DE Short=pHBA efflux pump protein B {ECO:0000255|HAMAP-Rule:MF_01545};
GN Name=aaeB {ECO:0000255|HAMAP-Rule:MF_01545}; OrderedLocusNames=STM3364;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Forms an efflux pump with AaeA. Could function as a metabolic
CC relief valve, allowing to eliminate certain compounds when they
CC accumulate to high levels in the cell. {ECO:0000255|HAMAP-
CC Rule:MF_01545}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01545}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01545}.
CC -!- SIMILARITY: Belongs to the aromatic acid exporter ArAE (TC 2.A.85)
CC family. {ECO:0000255|HAMAP-Rule:MF_01545}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006468; AAL22233.1; -; Genomic_DNA.
DR RefSeq; NP_462274.1; NC_003197.2.
DR RefSeq; WP_000510913.1; NC_003197.2.
DR AlphaFoldDB; Q8ZLP5; -.
DR STRING; 99287.STM3364; -.
DR PaxDb; Q8ZLP5; -.
DR EnsemblBacteria; AAL22233; AAL22233; STM3364.
DR GeneID; 1254887; -.
DR KEGG; stm:STM3364; -.
DR PATRIC; fig|99287.12.peg.3565; -.
DR HOGENOM; CLU_027647_0_0_6; -.
DR OMA; MITQACE; -.
DR PhylomeDB; Q8ZLP5; -.
DR BioCyc; SENT99287:STM3364-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046942; P:carboxylic acid transport; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR HAMAP; MF_01545; AaeB; 1.
DR InterPro; IPR006726; PHBA_efflux_AaeB/fusaric-R.
DR InterPro; IPR023706; PHBA_efflux_pump_AaeB.
DR PANTHER; PTHR30509:SF10; PTHR30509:SF10; 1.
DR Pfam; PF04632; FUSC; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..655
FT /note="p-hydroxybenzoic acid efflux pump subunit AaeB"
FT /id="PRO_0000210084"
FT TOPO_DOM 1..12
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 34..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 59..68
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 90..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 114..120
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 142..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 173..369
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 391..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 428..430
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 452..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 480..481
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TOPO_DOM 503..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 655 AA; 73646 MW; BF8404B010C70FD6 CRC64;
MGIFSIANQH IRFAVKLACA IVLALFIGFH FQLETPRWAV LTAAIVAAGP AFAAGGEPYS
GAIRYRGMLR IIGTFIGCIA ALIIIISMIR APLLMILVCC VWAGFCTWIS SLVRIENSYA
WGLSGYTALI IVITIQTEPL LTPQFALERC SEIVIGIGCA ILADLLFSPR SIKQEVDREL
DSLLVAQYQL MQLCIKHGDS EEVDNAWGDL VRRTAALEGM RSNLNMESSR WVRANRRLKA
LNTLSLTLIT QSCETYLIQN TRPELITDTF RELFETPVET VQDVHRQLKR MRRVIVWTGE
RETPVTLYSW VGAATRYLLL KRGVISNTKI SATEEEILQG EPVVKVESAE RHHAMVNFWR
TTLSCILGTL FWLWTGWTSG NGAMVMIAVV TSLAMRLPNP RMVCIDFIYG TLAALPLGLL
YFLVIIPNTQ QSMLLLCLSL AVLGFFIGIE VQKRRLGSMG ALASTINIIV LDNPMTFHFS
QFLDSALGQI VGCMLAFIVI LLVRDKSKDR TGRVLLNQFV SAAVSAMTTN VVRRKENRLP
ALYQQLFLLM NKFPGDLPKF RLALTMIIAH QRLRDAPIPV NEDLSVFHRQ LRRTADHVIS
AGSDDKRRRY FGQLLDELDI YQEKLRIWEA PPQVTEPVKR LTGMLHKYQN ALTDS
