ID   NUOB_PECCC              Reviewed;         224 AA.
AC   O85274;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 45.
DE   RecName: Full=NADH-quinone oxidoreductase subunit B;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit B;
DE   AltName: Full=NDH-1 subunit B;
GN   Name=nuoB;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora
OS   subsp. carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   MEDLINE=98305692; PubMed=9643539;
RX   DOI=10.1046/j.1365-2958.1998.00825.x;
RA   Harris S.J., Shih Y.L., Bentley S.D., Salmond G.P.C.;
RT   "The hexA gene of Erwinia carotovora encodes a LysR homologue and
RT   regulates motility and the expression of multiple virulence
RT   determinants.";
RL   Mol. Microbiol. 28:705-717(1998).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain.
CC       Couples the redox reaction to proton translocation (for every two
CC       electrons transferred, four hydrogen ions are translocated across
CC       the cytoplasmic membrane), and thus conserves the redox energy in
CC       a proton gradient (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits
CC       nuoB, CD, E, F, and G constitute the peripheral sector of the
CC       complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
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DR   EMBL; AF057063; AAC38641.1; -; Genomic_DNA.
DR   BRENDA; 1.6.99.5; 290410.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:HAMAP.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:HAMAP.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01356; -; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UbQ_OxRdtase_su-20kDa.
DR   InterPro; IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB.
DR   PANTHER; PTHR11995:SF2; NADH_DH_20kDa; 1.
DR   PANTHER; PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; NAD; Oxidoreductase; Quinone; Transport;
KW   Ubiquinone.
FT   CHAIN         1    224       NADH-quinone oxidoreductase subunit B.
FT                                /FTId=PRO_0000118772.
FT   METAL        67     67       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL        68     68       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       133    133       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       162    162       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   224 AA;  25606 MW;  D02202559740BC81 CRC64;
     MDYTLTRIEP DGENDRYPLQ RQEIVSDPLE QHVHRSVYMG KLEHALHDTV NWGRQNSLWP
     YNFGLSCCYV EMVTSFTAVH DVARFGAEVL RASPRQADFM VVAGTCFTKM APVIQRLYEQ
     MLEPKWVISM GACANSGGMY DIYSVVQGVD KFLPVDVYIP GCPPRPEAYM QALLLLKESI
     GKERRPLSWV VGEQGVYRAN MQSERERKRG ERIAVTNLRS PDEI
//