NORM_BURVI
ID NORM_BURVI Reviewed; 462 AA.
AC Q9F5N7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Multidrug resistance protein NorM;
DE AltName: Full=Multidrug-efflux transporter;
GN Name=norM;
OS Burkholderia vietnamiensis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=60552;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=CEP040;
RX PubMed=12399047; DOI=10.1111/j.1574-6968.2002.tb11403.x;
RA Fehlner-Gardiner C.C., Valvano M.A.;
RT "Cloning and characterization of the Burkholderia vietnamiensis norM gene
RT encoding a multi-drug efflux protein.";
RL FEMS Microbiol. Lett. 215:279-283(2002).
CC -!- FUNCTION: Multidrug efflux pump. Confers probably resistance to the
CC cationic peptide polymyxin B (PMB). {ECO:0000269|PubMed:12399047}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; AF312031; AAG27731.1; -; Genomic_DNA.
DR RefSeq; WP_011883895.1; NZ_UZVT01000001.1.
DR AlphaFoldDB; Q9F5N7; -.
DR SMR; Q9F5N7; -.
DR TCDB; 2.A.66.1.9; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PRIDE; Q9F5N7; -.
DR OMA; AAWFELF; -.
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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR002528; MATE_fam.
DR Pfam; PF01554; MatE; 2.
DR PIRSF; PIRSF006603; DinF; 1.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Antiport; Cell inner membrane; Cell membrane;
KW Ion transport; Membrane; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..462
FT /note="Multidrug resistance protein NorM"
FT /id="PRO_0000164213"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 462 AA; 47860 MW; 0CAFB2EC20652D11 CRC64;
MSHSGLTRTA AAPPSLSRHA VDTARLAAPL AIAQLSQMAM SVTDTVLLGS LGPDSLAAGG
LGANFFFVIV TVLQGVLSSV SVSVAHARGA QAEHRVPHIY WTGFVLSVLL AIPAVVALSL
SEPLLLMFHE PPTLAQHVGE YTGILRFAAL GSLIGVGLMR AFLPAIGAAR RLLWVSIGGI
GVNAVLNYGL IHGAYGLPRL GFLGSAVATT ITIWLTAFAL IWLLHGRARF RHFVSAARPK
LPMMGELIGI GWPVAITYGV ESTLFLATGL TVGVLGATAL AAHQIALNVA SVAFMVPLAI
GQAANVRVGY WIGAGDPVAA RHAGFVALGL GVAFMSLSGL VLILAPHAIV GLYLHLDDPA
NAATVSLAAS LLGIAAVFQI VDGMQTVGSG ALRGLRDTRI PMLAATFGYW GIGFPTGYWL
AFHAGLGARG LWWGLAAGLA SVAVLMAWRF HLKTSSLIAA PR