NORA_STAAU
ID NORA_STAAU Reviewed; 388 AA.
AC P0A0J7; P21191;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Quinolone resistance protein NorA;
GN Name=norA;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2174864; DOI=10.1128/jb.172.12.6942-6949.1990;
RA Yoshida H., Bogaki M., Nakamura S., Ubukata K., Konno M.;
RT "Nucleotide sequence and characterization of the Staphylococcus aureus norA
RT gene, which confers resistance to quinolones.";
RL J. Bacteriol. 172:6942-6949(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 230-388.
RC STRAIN=ATCC 21027 / 209-P;
RX PubMed=2173911; DOI=10.1016/0006-291x(90)91549-8;
RA Ohshita Y., Hiramatsu K., Yokota T.;
RT "A point mutation in norA gene is responsible for quinolone resistance in
RT Staphylococcus aureus.";
RL Biochem. Biophys. Res. Commun. 172:1028-1034(1990).
CC -!- FUNCTION: Involved in quinolone resistance. May constitute a membrane-
CC associated active efflux pump of hydrophilic quinolones.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; D90119; BAA14147.1; -; Genomic_DNA.
DR EMBL; M62960; AAB59089.1; -; Genomic_DNA.
DR PIR; A36242; A36242.
DR PIR; A37838; A37838.
DR RefSeq; WP_001041274.1; NZ_WYDB01000004.1.
DR AlphaFoldDB; P0A0J7; -.
DR SMR; P0A0J7; -.
DR BindingDB; P0A0J7; -.
DR ChEMBL; CHEMBL5114; -.
DR DrugCentral; P0A0J7; -.
DR TCDB; 2.A.1.2.10; the major facilitator superfamily (mfs).
DR OMA; LYADSFH; -.
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:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004734; Multidrug-R.
DR InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR01035; TCRTETA.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00880; 2_A_01_02; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..388
FT /note="Quinolone resistance protein NorA"
FT /id="PRO_0000173374"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 352
FT /note="D -> A (no quinolone resistance)"
FT CONFLICT 263
FT /note="M -> V (in Ref. 2; AAB59089)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="A -> D (in Ref. 2; AAB59089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 42265 MW; C36177EAEAADAC57 CRC64;
MNKQIFVLYF NIFLIFLGIG LVIPVLPVYL KDLGLTGSDL GLLVAAFALS QMIISPFGGT
LADKLGKKLI ICIGLILFSV SEFMFAVGHN FSVLMLSRVI GGMSAGMVMP GVTGLIADIS
PSHQKAKNFG YMSAIINSGF ILGPGIGGFM AEVSHRMPFY FAGALGILAF IMSIVLIHDP
KKSTTSGFQK LEPQLLTKIN WKVFITPVIL TLVLSFGLSA FETLYSLYTA DKVNYSPKDI
SIAITGGGIF GALFQIYFFD KFMKYFSELT FIAWSLLYSV VVLILLVFAN GYWSIMLISF
VVFIGFDMIR PAITNYFSNI AGERQGFAGG LNSTFTSMGN FIGPLIAGAL FDVHIEAPIY
MAIGVSLAGV VIVLIEKQHR AKLKEQNM