ID   NAPA_CAMC1              Reviewed;         926 AA.
AC   A7ZCK4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 14.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=Ccon26_06280; ORFNames=CCC13826_0868;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-2007) 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; CP000792; EAT97977.1; -; Genomic_DNA.
DR   RefSeq; YP_001466512.1; -.
DR   GeneID; 5597288; -.
DR   GenomeReviews; CP000792_GR; Ccon26_06280.
DR   KEGG; cco:CCC13826_0868; -.
DR   OMA; A7ZCK4; NMLYNIH.
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   InterPro; IPR017909; Twin_arg_translocation_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; 1.
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    926       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000073640.
FT   METAL        44     44       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        47     47       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        51     51       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        79     79       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   926 AA;  104218 MW;  04D4862157A3E725 CRC64;
     MNRRDFIKSA AASAACASAG IAVPSSLSAA NEAEKGWRWD KAACRFCGTG CGIMVATKDG
     KIVAVKGDPE APVNRGLNCI KGYFNAKIMY GEDRITHPLL RVNEKGEFDK KGKFKQVSWK
     QAFDVMEAQF RKTYDELGPH GVGVLGSGQY TIPEGYAAVK LMKGGFRSNS IDPNARHCMA
     SAVLGFMQVF GIDEPSGCFD DIELTDTVIA WGANMAEMHP ILWARVSDRK LSDPDRVKVV
     NLSTYSTRTS NLADIEIIFA PSSDLAIWNY IAREIVYNHP EMIDEEFVKK HCVFTAGPVD
     IGYGLRPDIH HKKYAPSELD TAATEKSKVL SEAEGVTLSY LGLKAGDTLE NKNAAKADAH
     WQITFEEFKK ALAPYTLDFT AKVAKGDPNE DINEFKKKLK ALADLYIEKN RKVVSFWTMG
     FNQHQRGTWV NEQAYMVHFL LGKQALPGSG AFSLTGQPSA CGTAREVGTF VHRLPADMVV
     GNPKHREITE KLWKLPAGTL SGTPGSHYVK MMRDLEDGKV KFIWVQVNNP WQNTANANHW
     IKAAREMDNF IVVSDPYPGI SAKVADLILP TAMIYEKWGA YGNAERRTQH WRQQVLPVGE
     AMPDIWQMLE FSKRFKLKDV WGEKKVNDKV TLPSVLEAAK AMGYSEEDTL FDVLFANEDA
     KKFSANDPIM ENYDNTEVFG DSRKVIGSDG KEFKGYGFFI HKYLWEEYRK FGVGHGHDLA
     DFDTYHRVRG LRWPVVDGKE TQWRFNTKFD PYAKKAAPND KFAFYGNKNA ALPTGDLKGV
     KNQEKTPLAN KAKIFFRPYM DPCEMPSKDY PFWLCTGRVL EHWHTGTMTM RVPELYRAVP
     EALCYMHEDD AKKLGVLQNE IVWVESRRGK VKARVDLKGR NKPPVGLVYV PFFDENVFIN
     KVCLDATCPI SKETDYKKCA VKIYKA
//