ID E3HS85_ACHXA Unreviewed; 393 AA.
AC E3HS85;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Periplasmic linker protein 1 {ECO:0000313|EMBL:ADP16031.1};
GN Name=bpeA1 {ECO:0000313|EMBL:ADP16031.1};
GN OrderedLocusNames=AXYL_02711 {ECO:0000313|EMBL:ADP16031.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP16031.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP16031.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP16031.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
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; CP002287; ADP16031.1; -; Genomic_DNA.
DR AlphaFoldDB; E3HS85; -.
DR STRING; 762376.AXYL_02711; -.
DR KEGG; axy:AXYL_02711; -.
DR eggNOG; COG0845; Bacteria.
DR HOGENOM; CLU_018816_2_1_4; -.
DR OrthoDB; 9783047at2; -.
DR Proteomes; UP000006876; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..393
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003171438"
FT DOMAIN 33..357
FT /note="Cation efflux system protein CusB"
FT /evidence="ECO:0000259|Pfam:PF00529"
FT DOMAIN 58..289
FT /note="RND efflux pump membrane fusion protein barrel-
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF16576"
SQ SEQUENCE 393 AA; 41312 MW; 4F7D118AFDD6F791 CRC64;
MWRSAAVVTL TASALTLAAC GKKQDAPQAG KPQVTVVTLA TQPVSLTTEL PGRTSPFRVA
EVRPQVNGIV QKRLFTEGGE VKAGQQLYQI DPALYQASLD SQKAALARAQ AQQKTAALLA
ERYKPLVATR AVSQQTYDNA VAARDQAAAD VLSAKAALDT ARINLVYTKV LSPIDGIIGR
SAVTEGALVT ANQTTALAAV QQIDPIYVDV TQSTVQLLRL QNALASGQLK KADGEQAALV
TLTLEDGSQY SQPGKLQFSE VTVDQGTGSV TLRAVFANPD RRLLPGMFVR ARLADGVAAD
GLLVPQRGVT RNQRGIPTAL VVNAKNQVEL RELKTDRAIG DKWLVTDGLA AGEKVIVEGL
QMVRPGAEVV ATEASAAAQP AQQPQAAAAA AKQ
//