AAEB_SHIBS
ID AAEB_SHIBS Reviewed; 655 AA.
AC Q31WA8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=SBO_3149;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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}.
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DR EMBL; CP000036; ABB67650.1; -; Genomic_DNA.
DR RefSeq; WP_000510930.1; NC_007613.1.
DR AlphaFoldDB; Q31WA8; -.
DR EnsemblBacteria; ABB67650; ABB67650; SBO_3149.
DR KEGG; sbo:SBO_3149; -.
DR HOGENOM; CLU_027647_0_0_6; -.
DR OMA; MITQACE; -.
DR Proteomes; UP000007067; Chromosome.
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:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046942; P:carboxylic acid transport; IEA:InterPro.
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; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..655
FT /note="p-hydroxybenzoic acid efflux pump subunit AaeB"
FT /id="PRO_0000300565"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01545"
SQ SEQUENCE 655 AA; 73535 MW; D2D421980A9B7633 CRC64;
MGIFSIANQH IRFAVKLATA IVLALFVGFH FQLETPRWAV LTAAIVAAGP AFAAGGEPYS
GAIRYRGFLR IIGTFIGCIA GLVIIIAMIR APLLMILVCC IWAGFCTWIS SLVRIENSYA
WGLAGYTALI IVITIQPEPL LTPQFAVERC SEIVIGIVCA IIADLLFSPR SIKQEVDREL
ESLLVAQYQL MQLCIKHGDG EVVDKAWGDL VRRTTGLQGM RSNLNMESSR WARANRRLKA
INTLSLTLIT QSCETYLIQN TRPELITDTF REFFDTPVET AQDVHKQLKR LRRVIAWTGE
RETPVTIYSW VAAATRYQLL KRGVISNTKI NATEEEILQG EPEVKVESAE RHHAMVNFWR
TTLSCILGTL FWLWTGWTSG SGAMVMIAVV TSLAMRLPNP RMVAIDFIYG TLAALPLGLL
YFLVIIPNTQ QSMLLLCISL AVLGFFLGIE VQQRLLGSMG ALASTINIIV LDNPMTFHFS
QFLDSALGQI VGCVLAFTVI LLVRDKSRDR TGRVLLNQFV SAAVSAMTTN VARRKENHLP
ALYQQLFLLM NKFPGDLPKF RLALTMIIAH QRLRDAPIPV NEDLSAFHRQ MRRTADHVIS
ARSDDKRRRY FGQLLEELEI YQEKLRIWQA PPQVTEPVHR LAGMLHKYQH ALTDS