ID   NAPA_CAMJ8              Reviewed;         924 AA.
AC   A8FLJ3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-NOV-2008, entry version 11.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=C8J_0731;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS   11828).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17873037; DOI=10.1128/JB.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M.,
RA   Nuijten P.J.M., van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
CC   -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC       (NAP). Only expressed at high levels during aerobic growth. NapAB
CC       complex receives electrons from the membrane-anchored tetraheme
CC       protein napC, thus allowing electron flow between membrane and
CC       periplasm. Essential function for nitrate assimilation and may
CC       have a role in anaerobic metabolism (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
CC       acceptor.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC   -!- COFACTOR: Binds 1 molybdenum ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups
CC       per subunit (By similarity).
CC   -!- SUBUNIT: Interacts with napB (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/napA/narB subfamily.
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DR   EMBL; CP000814; ABV52330.1; -; Genomic_DNA.
DR   RefSeq; YP_001482307.1; -.
DR   GeneID; 5617060; -.
DR   GenomeReviews; CP000814_GR; C8J_0731.
DR   KEGG; cju:C8J_0731; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:HAMAP.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:HAMAP.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:HAMAP.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01630; -; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_Fe4S4.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006657; MPT_dinuc_bd.
DR   InterPro; IPR010051; NO3_reductase_lsu_periplasm.
DR   InterPro; IPR006311; Tat.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   TIGRFAMs; TIGR01706; NAPA; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.
DR   PROSITE; PS51318; TAT; FALSE_NEG.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase;
KW   Periplasm; Signal; Transport.
FT   SIGNAL        1     30       Tat-type signal (Potential).
FT   CHAIN        31    924       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000073641.
FT   METAL        42     42       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        45     45       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        49     49       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        77     77       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   924 AA;  104900 MW;  7F5EA4A1C9176630 CRC64;
     MNRRDFIKNT AIASAASVAG LSVPSSMLGA QEEDWKWDKA VCRFCGTGCG IMIARKDGKI
     VATKGDPAAP VNRGLNCIKG YFNAKIMYGE DRLVMPLLRM NEKGEFDKKG KFQQVSWQRA
     FDEMEKQFKK AYNELGVTGI GIFGSGQYTI QEGYAALKLA KAGFRTNNID PNARHCMASA
     VVGFMQTFGV DEPSGCYDDI ELTDTIITWG ANMAEMHPIL WSRVSDRKLS NLDKVKVVNL
     STFSNRTSNI ADIEIIFKPN TDLAIWNYIA REIVYNHPEA MDMKFIKDHC VFATGYADIG
     YGMRNNPNHP KFKESEKDTV EKENVITLDD EEATSLSYLG VKAGDKFEMK HQGVADKNWE
     ISFEEFKKGL APYTLEYTAK VAKGDDNESL EDFKKKLQEL ANLYIEKNRK VVSFWTMGFN
     QHTRGSWVNE QAYMVHFLLG KQAKPGSGAF SLTGQPSACG TAREVGTFSH RLPADMVVAN
     PKHREISEKI WKVPAKTINP KPGSPYLNIM RDLEDGKIKF AWVQVNNPWQ NTANANHWIA
     AAREMDNFIV VSDCYPGISA KVADLILPSA MIYEKWGAYG NAERRTQHWK QQVLPVGAAM
     SDTWQILEFA KRFKLKEVWK EQKVDNKLTL PSVLEEAKAM GYSEDDTLFD VLFANKEAKS
     FNPNDAIAKG FDNTDVKGDE RKIQGSDGKE FAGYGFFVQK YLWEEYRKFG LGHGHDLADF
     DTYHKVRGLR WPVVNGKETQ WRFNTKFDYY AKKAAPNSDF AFYGDFNKML TNGDLIAPKD
     EKEHSIKNKA KIFFRPFMKA PERPSKEYPF WLATGRVLEH WHSGTMTMRV PELYRAVPEA
     LCYMSEKDGE KLGLNQGDLV WVESRRGKVK ARVDMRGRNK PPVGLVYVPW FDENVYINKV
     TLDATCPLSK QTDFKKCAVK IYKA
//