ID A0A0H2VTA2_SHIFL Unreviewed; 397 AA.
AC A0A0H2VTA2; A0A2G3EPG0; Q7UDH9; Q83SE9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acriflavin resistance protein AcrA {ECO:0000313|EMBL:AAN42063.2};
GN Name=acrA {ECO:0000313|EMBL:AAN42063.2};
GN OrderedLocusNames=SF0408 {ECO:0000313|EMBL:AAN42063.2};
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623 {ECO:0000313|EMBL:AAN42063.2, ECO:0000313|Proteomes:UP000001006};
RN [1] {ECO:0000313|EMBL:AAN42063.2, ECO:0000313|Proteomes:UP000001006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a {ECO:0000313|Proteomes:UP000001006};
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004519}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004519}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477}.
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DR EMBL; AE005674; AAN42063.2; -; Genomic_DNA.
DR RefSeq; NP_706356.2; NC_004337.2.
DR RefSeq; WP_011069267.1; NZ_WPGW01000015.1.
DR AlphaFoldDB; A0A0H2VTA2; -.
DR SMR; A0A0H2VTA2; -.
DR PaxDb; 198214-SF0408; -.
DR GeneID; 1027728; -.
DR KEGG; sfl:SF0408; -.
DR PATRIC; fig|198214.7.peg.468; -.
DR Proteomes; UP000001006; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProt.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.420.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR InterPro; IPR043602; CusB_dom_1.
DR InterPro; IPR032317; HlyD_D23.
DR InterPro; IPR006143; RND_pump_MFP.
DR NCBIfam; TIGR01730; RND_mfp; 1.
DR PANTHER; PTHR30158; ACRA/E-RELATED COMPONENT OF DRUG EFFLUX TRANSPORTER; 1.
DR PANTHER; PTHR30158:SF3; MULTIDRUG EFFLUX PUMP SUBUNIT ACRA-RELATED; 1.
DR Pfam; PF00529; CusB_dom_1; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000001006};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..397
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030007328"
FT DOMAIN 38..360
FT /note="Cation efflux system protein CusB"
FT /evidence="ECO:0000259|Pfam:PF00529"
FT DOMAIN 63..293
FT /note="RND efflux pump membrane fusion protein barrel-
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF16576"
FT REGION 377..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 42153 MW; 53BACFDCACAD29F1 CRC64;
MNKNRGFTPL AVVLMLSGSL ALTGCDDKQA QQGGQQMPAV GVVTVKTEPL QITTELPGRT
SAYRIAEVRP QVSGIILKRN FKEGSDIEAG VSLYQIDPAT YQATYDSAKG DLAKAQAAAN
IAQLTVNRYQ KLLGTQYISK QGYDQALADA QQANAAVTAA KAAVETARIN LAYTKVTSPI
SGRIGKSNVT EGALVQNGQA TVLATVQQLD PIYVDVTQSS NDFLRLKQEL ANGTLKQENG
KAKVSLITSD GIKFPQDGTL EFSDVTVDQT TGSITLRAIF PNPDHTLLPG MFVRARLEEG
LNPNAILVPQ QGVTRTPRGD ATVLVVGADD KVETRPIVAS QAIGDKWLVT EGLKAGDRVV
ISGLQKVRPG VQVKAQEVTA DNNQQAASGA QPEQSKS
//
