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Copper-containing nitrite reductase (EC 1.7.2.1) (Major outer membrane protein Pan 1)

 ANIA_NEIGO              Reviewed;         392 AA.
Q02219;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
05-JUL-2017, entry version 105.
RecName: Full=Copper-containing nitrite reductase;
EC=1.7.2.1;
AltName: Full=Major outer membrane protein Pan 1;
Flags: Precursor;
Name=aniA;
Neisseria gonorrhoeae.
Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
Neisseriaceae; Neisseria.
NCBI_TaxID=485;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=R10;
PubMed=1383156;
Hoehn G.T., Clark V.L.;
"Isolation and nucleotide sequence of the gene (aniA) encoding the
major anaerobically induced outer membrane protein of Neisseria
gonorrhoeae.";
Infect. Immun. 60:4695-4703(1992).
[2]
PALMITOYLATION AT CYS-19, AND DIACYLGLYCEROL AT CYS-19.
STRAIN=ATCC 33084 / F62 / M-1914;
PubMed=1398981;
Hoehn G.T., Clark V.L.;
"The major anaerobically induced outer membrane protein of Neisseria
gonorrhoeae, Pan 1, is a lipoprotein.";
Infect. Immun. 60:4704-4708(1992).
[3]
FUNCTION, AND INDUCTION.
STRAIN=MS11;
PubMed=9413436; DOI=10.1007/s004380050597;
Mellies J., Jose J., Meyer T.F.;
"The Neisseria gonorrhoeae gene aniA encodes an inducible nitrite
reductase.";
Mol. Gen. Genet. 256:525-532(1997).
[4]
TRANSCRIPTIONAL REGULATION BY FNR AND NARP.
STRAIN=ATCC 33084 / F62 / M-1914;
PubMed=9882668;
Householder T.C., Belli W.A., Lissenden S., Cole J.A., Clark V.L.;
"cis- and trans-acting elements involved in regulation of aniA, the
gene encoding the major anaerobically induced outer membrane protein
in Neisseria gonorrhoeae.";
J. Bacteriol. 181:541-551(1999).
[5]
PROTECTION AGAINST KILLING BY HUMAN SERA.
STRAIN=ATCC 33084 / F62 / M-1914;
PubMed=10858263; DOI=10.1128/IAI.68.7.4368-4369.2000;
Cardinale J.A., Clark V.L.;
"Expression of AniA, the major anaerobically induced outer membrane
protein of Neisseria gonorrhoeae, provides protection against killing
by normal human sera.";
Infect. Immun. 68:4368-4369(2000).
[6]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 42-364 IN COMPLEX WITH
SUBSTRATE AND COPPER IONS, AND SUBUNIT.
PubMed=11827480; DOI=10.1006/jmbi.2001.5251;
Boulanger M.J., Murphy M.E.P.;
"Crystal structure of the soluble domain of the major anaerobically
induced outer membrane protein (AniA) from pathogenic Neisseria: a new
class of copper-containing nitrite reductases.";
J. Mol. Biol. 315:1111-1127(2002).
-!- FUNCTION: Catalyzes the reduction of nitrite to nitric oxide (NO),
probably with azurin as electron donor. Essential for growth and
survival in oxygen-depleted environments. Can also provide
protection against killing by normal human sera.
{ECO:0000269|PubMed:9413436}.
-!- CATALYTIC ACTIVITY: Nitric oxide + H(2)O + ferricytochrome c =
nitrite + ferrocytochrome c + 2 H(+).
-!- COFACTOR:
Name=Cu(+); Xref=ChEBI:CHEBI:49552;
Note=Binds 1 Cu(+) ion.;
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Note=Binds 1 Cu(2+) ion.;
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11827480}.
-!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-
anchor {ECO:0000305}.
-!- INDUCTION: By anaerobic and microaerophilic conditions in the
presence of nitrite. Regulated by the gonococcal fnr and NarP
homologs. {ECO:0000269|PubMed:1383156, ECO:0000269|PubMed:9413436,
ECO:0000269|PubMed:9882668}.
-!- PTM: Palmitoylated. {ECO:0000269|PubMed:1398981}.
-!- MISCELLANEOUS: Undetected during aerobic growth.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M97926; AAA25462.1; -; Genomic_DNA.
PIR; A49208; A49208.
RefSeq; WP_003700168.1; NZ_JPOZ01000058.1.
PDB; 1KBV; X-ray; 1.95 A; A/B/C/D/E/F=42-364.
PDB; 1KBW; X-ray; 2.40 A; A/B/C/D/E/F=42-364.
PDBsum; 1KBV; -.
PDBsum; 1KBW; -.
ProteinModelPortal; Q02219; -.
SMR; Q02219; -.
PATRIC; fig|485.42.peg.2461; -.
eggNOG; ENOG4105CEI; Bacteria.
eggNOG; COG2132; LUCA.
EvolutionaryTrace; Q02219; -.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:UniProtKB-EC.
GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
Gene3D; 2.60.40.420; -; 2.
InterPro; IPR011707; Cu-oxidase_3.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR001287; NO2-reductase_Cu.
Pfam; PF07732; Cu-oxidase_3; 1.
PRINTS; PR00695; CUNO2RDTASE.
SUPFAM; SSF49503; SSF49503; 2.
TIGRFAMs; TIGR02376; Cu_nitrite_red; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Cell outer membrane; Copper; Lipoprotein; Membrane;
Metal-binding; Oxidoreductase; Palmitate; Repeat; Signal.
SIGNAL 1 18 {ECO:0000305}.
CHAIN 19 392 Copper-containing nitrite reductase.
/FTId=PRO_0000002997.
DOMAIN 101 195 Plastocyanin-like 1.
DOMAIN 245 346 Plastocyanin-like 2.
REPEAT 368 372 1.
REPEAT 373 377 2.
REPEAT 378 382 3.
REPEAT 383 387 4.
REGION 368 387 4 X 5 AA tandem repeats of A-A-S-A-P.
METAL 134 134 Copper 1; type 1.
METAL 139 139 Copper 2; type 2.
METAL 174 174 Copper 2; type 2.
METAL 175 175 Copper 1; type 1.
METAL 183 183 Copper 1; type 1.
METAL 188 188 Copper 1; type 1.
METAL 329 329 Copper 2; type 2.
BINDING 139 139 Substrate. {ECO:0000269|PubMed:11827480}.
BINDING 280 280 Substrate. {ECO:0000269|PubMed:11827480}.
LIPID 19 19 N-palmitoyl cysteine.
{ECO:0000305|PubMed:1398981}.
LIPID 19 19 S-diacylglycerol cysteine.
{ECO:0000305|PubMed:1398981}.
STRAND 56 58 {ECO:0000244|PDB:1KBV}.
STRAND 78 93 {ECO:0000244|PDB:1KBV}.
STRAND 96 103 {ECO:0000244|PDB:1KBV}.
STRAND 106 108 {ECO:0000244|PDB:1KBV}.
STRAND 111 115 {ECO:0000244|PDB:1KBV}.
STRAND 119 126 {ECO:0000244|PDB:1KBV}.
HELIX 144 147 {ECO:0000244|PDB:1KBV}.
TURN 148 151 {ECO:0000244|PDB:1KBV}.
STRAND 157 164 {ECO:0000244|PDB:1KBV}.
STRAND 169 174 {ECO:0000244|PDB:1KBV}.
HELIX 180 185 {ECO:0000244|PDB:1KBV}.
STRAND 189 195 {ECO:0000244|PDB:1KBV}.
STRAND 204 214 {ECO:0000244|PDB:1KBV}.
STRAND 216 218 {ECO:0000244|PDB:1KBV}.
STRAND 224 226 {ECO:0000244|PDB:1KBV}.
HELIX 230 235 {ECO:0000244|PDB:1KBV}.
STRAND 239 243 {ECO:0000244|PDB:1KBV}.
TURN 247 250 {ECO:0000244|PDB:1KBV}.
HELIX 252 254 {ECO:0000244|PDB:1KBV}.
STRAND 256 259 {ECO:0000244|PDB:1KBV}.
STRAND 262 274 {ECO:0000244|PDB:1KBV}.
STRAND 277 282 {ECO:0000244|PDB:1KBV}.
STRAND 286 290 {ECO:0000244|PDB:1KBV}.
HELIX 291 293 {ECO:0000244|PDB:1KBV}.
STRAND 300 306 {ECO:0000244|PDB:1KBV}.
STRAND 310 318 {ECO:0000244|PDB:1KBV}.
STRAND 322 330 {ECO:0000244|PDB:1KBV}.
HELIX 332 336 {ECO:0000244|PDB:1KBV}.
STRAND 340 347 {ECO:0000244|PDB:1KBV}.
TURN 351 353 {ECO:0000244|PDB:1KBV}.
SEQUENCE 392 AA; 40954 MW; A4707CC87B923C97 CRC64;
MKRQALAAMI ASLFALAACG GEQAAQAPAE TPAASAEAAS SAAQATAETP AGELPVIDAV
TTHAPEVPPA IDRDYPAKVR VKMETVEKTM KMDDGVEYRY WTFDGDVPGR MIRVREGDTV
EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA TFTAPGRTST FSFKALQPGL YIYHCAVAPV
GMHIANGMYG LILVEPKEGL PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY
VVFNGHVGSI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN
VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN PEIMTQKLSD
TAYAGSGAAS APAASAPAAS APAASASEKS VY


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