ID   NAPA_CAMJJ              Reviewed;         923 AA.
AC   A1VZC8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=CJJ81176_0801;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000538; EAQ72370.1; -; Genomic_DNA.
DR   RefSeq; YP_001000469.1; -.
DR   GeneID; 4683033; -.
DR   GenomeReviews; CP000538_GR; CJJ81176_0801.
DR   KEGG; cjj:CJJ81176_0801; -.
DR   TIGR; CJJ81176_0801; -.
DR   OMA; A1VZC8; ERRTQAW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:UniProtKB-KW.
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    923       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000069714.
FT   METAL        41     41       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        44     44       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        48     48       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        76     76       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   923 AA;  104771 MW;  43A93C661081EE05 CRC64;
     MNRRDFIKNT AIASAASVAG LSVPSSMLGA QEDWKWDKAV CRFCGTGCGI MIARKDGKIV
     ATKGDPAAPV NRGLNCIKGY FNAKIMYGED RLVMPLLRMN EKGEFDKKGK FQQVSWQRAF
     DEMEKQFKKA YNELGVTGIG IFGSGQYTIQ EGYAALKLAK AGFRTNNIDP NARHCMASAV
     VGFMQTFGVD EPSGCYDDIE LTDTIITWGA NMAEMHPILW SRVSDRKLSN LDKVKVVNLS
     TFSNRTSNIA DIEIIFKPNT DLAIWNYIAR EIVYNHPEAM DMKFIKDHCV FATGYADIGY
     GMRNNPNHPK FKESEKDTVE KENVITLDDE EAASLSYLGV KAGDKFEMKH QGVADKNWEI
     SFEEFKKGLA PYTLEYTAKV AKGDDNESLE DFKKKLQELA NLYIEKNRKV VSFWTMGFNQ
     HTRGSWVNEQ AYMVHFLLGK QAKPGSGAFS LTGQPSACGT AREVGTFSHR LPADMVVANP
     KHREISEKIW KVPAKTINPK PGSPYLNIMR DLEDGKIKFA WVQVNNPWQN TANANHWIAA
     AREMDNFIVV SDCYPGISAK VADLILPSAM IYEKWGAYGN AERRTQHWKQ QVLPVGAAMS
     DTWQILEFAK RFKLKEVWKE QKVDNKLTLP SVLEEAKAMG YSEDDTLFDV LFANKEAKSF
     NPNDAIAKGF DNTDVKGDER KIQGSDGKEF TGYGFFVQKY LWEEYRKFGL GHGHDLADFD
     TYHKVRGLRW PVVNGKETQW RFNTKFDYYA KKAAPNSDFA FYGDFNKMLT NGDLIAPKDE
     KEHSIKNKAK IFFRPFMKAP ERPSKEYPFW LATGRVLEHW HSGTMTMRVP ELYRAVPEAL
     CYMSEKDGEK LGLNQGDLVW VESRRGKVKA RVDMRGRNKP PVGLVYVPWF DENVYINKVT
     LDATCPLSKQ TDFKKCAVKI YKA
//