Q9K1C2 (NUOB_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH-quinone oxidoreductase subunit B
EC=1.6.99.5

Alternative name(s):
NADH dehydrogenase I subunit B
NDH-1 subunit B

Gene names

Name:	nuoB
Ordered Locus Names:	NMB0242

Organism

Neisseria meningitidis serogroup B

Taxonomic identifier

491 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient By similarity. HAMAP MF_01356
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP MF_01356
Cofactor	Binds 1 4Fe-4S cluster By similarity. HAMAP MF_01356
Subunit structure	NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_01356.
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 160	160	NADH-quinone oxidoreductase subunit B HAMAP MF_01356		PRO_0000358430
Sites
	Metal binding	37	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	38	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	102	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	132	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9K1C2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F1616423A8D799AF	FASTA	160	17,630
	10 20 30 40 50 60 MGIEGVLKKG FITTSADTVL NYMRTGSLWP VTFGLACCAV EMMHAGMARY DLDRFGIIFR 70 80 90 100 110 120 PSPRQADLMI VAGTLTNKMA PALRRVYDQL AEPRWVLSMG SCANGGGYYH YSYSVVRGAD 130 140 150 160 RVVPVDVYVP GCPPTAEALI YGLIQLQQKI KRTSTIARDE

References

[1]

"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C. Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002098 Genomic DNA. Translation: AAF40696.1.
PIR	H81221.
RefSeq	NP_273298.1. NC_003112.2.
3D structure databases
ProteinModelPortal	Q9K1C2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBNEIT00000009540; EBNEIP00000009160; EBNEIG00000009540.
GeneID	902353.
GenomeReviews	Gene locus NMB0242 in contig AE002098_GR.
KEGG	nme:NMB0242.
PATRIC	20355560. VBINeiMen85645_0304.
TIGR	NMB0242.
Phylogenomic databases
GeneTree	EBGT00050000020904.
HOGENOM	HBG553221.
OMA	QNKIRRT.
ProtClustDB	PRK06411.
Enzyme and pathway databases
BioCyc	NMEN122586:NMB_0242-MONOMER.
Family and domain databases
HAMAP	MF_01356. NDH1_NuoB. [Tree]
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UQ_OxRdtase_20Kd_su. IPR014406. NiFe-hyd_3_ssu/Q_oxred_NuoB. [Graphical view]
Gene3D	G3DSA:3.40.50.700. G3DSA:3.40.50.700. 1 hit.
KO	K00331.
PANTHER	PTHR11995. NiFe_hyd_3_ssu/Q_oxred_NuoB. 1 hit.
Pfam	PF01058. Oxidored_q6. 1 hit. [Graphical view]
TIGRFAMs	TIGR01957. NuoB_fam. 1 hit.
PROSITE	PS01150. COMPLEX1_20K. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOB_NEIMB

Accession

Primary (citable) accession number: Q9K1C2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program