Reviewed, UniProtKB/Swiss-Prot Q5HV12 (NAPA_CAMJR)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	CJE0871

Organism

Campylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]

Taxonomic identifier

195099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	924 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein napC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism By similarity.
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor.
Cofactor	Binds 1 4Fe-4S cluster By similarity. Binds 1 molybdenum ion per subunit By similarity. Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit By similarity.
Subunit structure	Interacts with napB By similarity.
Subcellular location	PeriplasmBy similarity.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/napA/narB subfamily.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Periplasm
Domain	Signal
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: HAMAP electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP molybdenum ion binding Inferred from electronic annotation. Source: InterPro nitrate reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	Tat-type signal Potential
	Chain	31 – 924	894	Periplasmic nitrate reductase		PRO_0000045981
Sites
	Metal binding	42	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	45	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	49	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	77	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HV12-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 9DA5E87E0263BC9A	FASTA	924	104,944
	10 20 30 40 50 60 MNRRDFIKNT AIASAASVAG LSVPSSMLGA QEEDWKWDKA VCRFCGTGCG IMIARKDGKI 70 80 90 100 110 120 VATKGDPAAP VNRGLNCIKG YFNAKIMYGE DRLVMPLLRM NEKGEFDKKG KFQQVSWQRA 130 140 150 160 170 180 FDEMEKQFKK AYNELGVTGI GIFGSGQYTI QEGYAALKLA KAGFRTNNID PNARHCMASA 190 200 210 220 230 240 VVGFMQTFGV DEPSGCYDDI ELTDTIITWG ANMAEMHPIL WSRVSDRKLS NLDKVKVVNL 250 260 270 280 290 300 STFSNRTSNI ADIEIIFKPN TDLAIWNYIA REIVYNHPEA MDMKFIKDHC VFATGYADIG 310 320 330 340 350 360 YGMRNNPNHP KFKESEKDTV EKENVITLDD EEATSLSYLG VKAGDKFEMK HQGVADKNWE 370 380 390 400 410 420 ISFDEFKKGL APYTLEYTAR VAKGDDNESL EDFKKKLQEL ANLYIEKNRK VVSFWTMGFN 430 440 450 460 470 480 QHTRGSWVNE QAYMVHFLLG KQAKPGSGAF SLTGQPSACG TAREVGTFSH RLPADMVVAN 490 500 510 520 530 540 PKHREISEKI WKVPAKTINP KPGSPYLNIM RDLEDGKIKF AWVQVNNPWQ NTANANHWIA 550 560 570 580 590 600 AAREMDNFIV VSDCYPGISA KVADLILPSA MIYEKWGAYG NAERRTQHWK QQVLPVGAAM 610 620 630 640 650 660 SDTWQILEFA KRFKLKEVWK EQKVDNKLTL PSVLEEAKAM GYSEDDTLFD VLFANKEAKS 670 680 690 700 710 720 FNPNDAIAKG FDNTDVKGDE RKIQGSDGKE FTGYGFFVQK YLWEEYRKFG LGHGHDLADF 730 740 750 760 770 780 DTYHKVRGLR WPVVNGKETQ WRFNTKFDYY AKKAAPNSDF AFYGDFNKML TNGDLIAPKD 790 800 810 820 830 840 EKEHSIKNKA KIFFRPFMKA PERPSKEYPF WLATGRVLEH WHSGTMTMRV PELYRAVPEA 850 860 870 880 890 900 LCYMSEKDGE KLGLNQGDLV WVESRRGKVK ARVDMRGRNK PPVGLVYVPW FDENVYINKV 910 920 TLDATCPLSK QTDFKKCAVK IYKA

References

[1]

"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species." Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. , Badger J.H., Fraser C.M., Nelson K.E. PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000025 Genomic DNA. Translation: AAW35208.1.
RefSeq	YP_178873.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3231384.
GenomeReviews	Gene locus CJE0871 in contig CP000025_GR.
KEGG	cjr:CJE0871.
TIGR	CJE0871.
Phylogenomic databases
HOGENOM	Q5HV12.
Enzyme and pathway databases
BioCyc	CJEJ195099:CJE_0871-MON.
Family and domain databases
HAMAP	MF_01630. [Tree]
InterPro	IPR009010. Asp_de-COase-like_fold. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4. IPR006655. Mopterin_OxRdtase_prok_CS. IPR006657. MPT_dinuc_bd. IPR010051. NO3_reductase_lsu_periplasm. IPR006311. Tat. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
Pfam	PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR01706. NAPA. 1 hit. TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. 1 hit. PS00490. MOLYBDOPTERIN_PROK_2. False negative. PS00932. MOLYBDOPTERIN_PROK_3. False negative. PS51318. TAT. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAPA_CAMJR

Accession

Primary (citable) accession number: Q5HV12

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	February 15, 2005
Last modified:	November 25, 2008
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)