ID Q2L1H2_BORA1 Unreviewed; 396 AA.
AC Q2L1H2;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Acriflavine resistance protein A {ECO:0000313|EMBL:CAJ49261.1};
GN Name=acrA {ECO:0000313|EMBL:CAJ49261.1};
GN Synonyms=mtcA {ECO:0000313|EMBL:CAJ49261.1};
GN OrderedLocusNames=BAV1653 {ECO:0000313|EMBL:CAJ49261.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49261.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ49261.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ49261.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49261.1; -; Genomic_DNA.
DR RefSeq; WP_012417322.1; NC_010645.1.
DR AlphaFoldDB; Q2L1H2; -.
DR STRING; 360910.BAV1653; -.
DR GeneID; 41393507; -.
DR KEGG; bav:BAV1653; -.
DR eggNOG; COG0845; Bacteria.
DR HOGENOM; CLU_018816_2_1_4; -.
DR OrthoDB; 9783047at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042221; P:response to chemical; 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:UP000001977};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..396
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004211890"
FT DOMAIN 36..361
FT /note="Cation efflux system protein CusB"
FT /evidence="ECO:0000259|Pfam:PF00529"
FT DOMAIN 61..293
FT /note="RND efflux pump membrane fusion protein barrel-
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF16576"
SQ SEQUENCE 396 AA; 41841 MW; 1E11AA8746F67AB8 CRC64;
MKSKTQIGRI VFSTVALALA LAGCGKEQAA PAQGKPQVGV VTLKPQAVAL STELPGRTSA
YRIAEVRPQV SGIVQQRMFT EGREVRANQQ LYQIDPSLYQ ASYDSAKAAL ARAQAQARTA
ALLVDRYKPL VTSRAVSQQT YDNAVAARDQ ANADVLAAKA ALETARINLV YTKVLSPIGG
IVGRSLVTEG ALVTANQAAA IASVQQIDPI YVDVTQSSVQ LLRLKQALAS GQLQQDDGAQ
AAKVTLVLED GSTYAEPGKL EFSEVTVDPS TGSVTLRALF PNPRHQLLPG MFVRANLAQG
VANEGLLVPQ RGVTRNQRGL PTALVVNADN KVELRELRTD RTVGDHWLVT QGLAAGDRVI
VEGLQSVRPG AEVNAKEFQA SAAAPAGQNG QSPVGK
//
