ID   NAPA_CAMFF              Reviewed;         925 AA.
AC   A0RQ36;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=CFF8240_1161;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-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; CP000487; ABK82549.1; -; Genomic_DNA.
DR   RefSeq; YP_892319.1; -.
DR   GeneID; 4539058; -.
DR   GenomeReviews; CP000487_GR; CFF8240_1161.
DR   KEGG; cff:CFF8240_1161; -.
DR   NMPDR; fig|360106.5.peg.1114; -.
DR   TIGR; CFF8240_1161; -.
DR   OMA; A0RQ36; 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   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    925       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000069712.
FT   METAL        43     43       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        46     46       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        50     50       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        78     78       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   925 AA;  104255 MW;  6421C720F2CE60BB CRC64;
     MDRREFIKSS AAAAACSAAG IAVPSSLSAA ENQDGWRWDK SACRFCGTGC GIMVATKNGK
     IVAVKGDPLA PVNRGLNCIK GYFNAKIMYG EDRITKPLLR VNANGEFDKK GKFQEVSWKR
     AFDEMEKQFR KTYAELGPTG IGVFGSGQYT IQEGYAISKL IKGGFRSHNI DPNARHCMAS
     AVVGFMQTFG IDEPAGCYDD IELTDTIVTW GANMAEMHPI LWSRVSDRKL QNSDKVKVVN
     LSTYSTRTSN IADIEIIFTP HTDLAIWNYI AREIVYNHPE AIDEEFVKAN CVFTTGPVDI
     GYGMRANIKH PKYLPSELDT AAKEKSTVLS ENEGVTLAYL GMKAGDTLEN KSTGAPDKHW
     IIQYEDFKKA LAPYTLDFVA KLAKGDPNED LEEFKKKLKA LADLYIEKNR KVVSFWTMGM
     NQHTRGVWVN EQSYMVHFLL GKQAKPGSGA FSLTGQPSAC GTAREVGTFS HRLPADMVVA
     NPKHREITEK IWKIPAGTIN PKPGAPYMKI MRDLEDGKVK FVWVHVNNPW QNSANANHWI
     KAAREMDNFI VVSDPYPGIS AKVGDLILPT AMIYEKWGAY GNAERRTQHW RQQVLPVGDA
     MSDTWQYMEF AKRFKLKDFW GEVKVDGKLT LPNVLDKAVA MGYNPENTLF EVLFANKSAM
     KFSSDDKIMA GYDNTEVFGD SRNVVGSDGN VFKGYGFFVQ KYLWEEYREF GLGHGHDLAD
     FDTYHKVRGL RWPVVDGKET LWRFNTKYDV YAKKDNPNGD FSFYGNKNGA LVTGDLAKAT
     SKEKEALKSR AKIFFRPYMD PPEMPSKDYP LWLCTGRVLE HWHSGTMTMR VPELYRAVPE
     ALCFMNEIDG NKFGIKQNDI IWVESRRGKV KARVDFRGRN KPAEGLIYVP WFDENVFINK
     VCLDATDPLS KQTDFKKCAV KIYKA
//