Q02219 (ANIA_NEIGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Copper-containing nitrite reductase
EC=1.7.2.1

Alternative name(s):
Major outer membrane protein Pan 1

Gene names

Name:

aniA

Organism

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.3
Catalytic activity	Nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+.
Cofactor	Binds 1 Cu+ ion. Binds 1 Cu2+ ion.
Subunit structure	Homotrimer. Ref.6
Subcellular location	Cell outer membrane; Lipid-anchor Probable.
Induction	By anaerobic and microaerophilic conditions in the presence of nitrite. Regulated by the gonococcal fnr and NarP homologs. Ref.1 Ref.3 Ref.4
Post-translational modification	Palmitoylated. Ref.2
Miscellaneous	Undetected during aerobic growth.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 2 plastocyanin-like domains.

Ontologies

Keywords
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Lipoprotein Palmitate
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	nitrogen compound metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro nitrite reductase (NO-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Probable

Chain

19 – 392

374

Copper-containing nitrite reductase

PRO_0000002997

Regions

Domain

101 – 195

95

Plastocyanin-like 1

Domain

245 – 346

102

Plastocyanin-like 2

Repeat

368 – 372

5

1

Repeat

373 – 377

5

2

Repeat

378 – 382

5

3

Repeat

383 – 387

5

4

Region

368 – 387

20

4 X 5 AA tandem repeats of A-A-S-A-P

Sites

Metal binding

134

1

Copper 1; type 1

Metal binding

139

1

Copper 2; type 2

Metal binding

174

1

Copper 2; type 2

Metal binding

175

1

Copper 1; type 1

Metal binding

183

1

Copper 1; type 1

Metal binding

188

1

Copper 1; type 1

Metal binding

329

1

Copper 2; type 2

Binding site

139

1

Substrate

Binding site

280

1

Substrate

Amino acid modifications

Lipidation

19

1

N-palmitoyl cysteine Probable

Lipidation

19

1

S-diacylglycerol cysteine Probable

Secondary structure

1

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392

Helix Strand Turn

Details...

Beta strand

56 – 58

3

Beta strand

78 – 93

16

Beta strand

96 – 103

8

Beta strand

106 – 108

3

Beta strand

111 – 115

5

Beta strand

119 – 126

8

Helix

144 – 147

4

Turn

148 – 151

4

Beta strand

157 – 164

8

Beta strand

169 – 174

6

Helix

180 – 185

6

Beta strand

189 – 195

7

Beta strand

204 – 214

11

Beta strand

216 – 218

3

Beta strand

224 – 226

3

Helix

230 – 235

6

Beta strand

239 – 243

5

Turn

247 – 250

4

Helix

252 – 254

3

Beta strand

256 – 259

4

Beta strand

262 – 274

13

Beta strand

277 – 282

6

Beta strand

286 – 290

5

Helix

291 – 293

3

Beta strand

300 – 306

7

Beta strand

310 – 318

9

Beta strand

322 – 330

9

Helix

332 – 336

5

Beta strand

340 – 347

8

Turn

351 – 353

3

Sequences

	Sequence		Length	Mass (Da)
	Q02219 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: A4707CC87B923C97	FASTA	392	40,954
	10 20 30 40 50 60 MKRQALAAMI ASLFALAACG GEQAAQAPAE TPAASAEAAS SAAQATAETP AGELPVIDAV 70 80 90 100 110 120 TTHAPEVPPA IDRDYPAKVR VKMETVEKTM KMDDGVEYRY WTFDGDVPGR MIRVREGDTV 130 140 150 160 170 180 EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA TFTAPGRTST FSFKALQPGL YIYHCAVAPV 190 200 210 220 230 240 GMHIANGMYG LILVEPKEGL PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY 250 260 270 280 290 300 VVFNGHVGSI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN 310 320 330 340 350 360 VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN PEIMTQKLSD 370 380 390 TAYAGSGAAS APAASAPAAS APAASASEKS VY

References

[1]	"Isolation and nucleotide sequence of the gene (aniA) encoding the major anaerobically induced outer membrane protein of Neisseria gonorrhoeae." Hoehn G.T., Clark V.L. Infect. Immun. 60:4695-4703(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: R10.
[2]	"The major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, Pan 1, is a lipoprotein." Hoehn G.T., Clark V.L. Infect. Immun. 60:4704-4708(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-19, DIACYLGLYCEROL AT CYS-19. Strain: ATCC 33084 / F62 / M-1914.
[3]	"The Neisseria gonorrhoeae gene aniA encodes an inducible nitrite reductase." Mellies J., Jose J., Meyer T.F. Mol. Gen. Genet. 256:525-532(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION. Strain: MS11.
[4]	"cis- and trans-acting elements involved in regulation of aniA, the gene encoding the major anaerobically induced outer membrane protein in Neisseria gonorrhoeae." Householder T.C., Belli W.A., Lissenden S., Cole J.A., Clark V.L. J. Bacteriol. 181:541-551(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION BY FNR AND NARP. Strain: ATCC 33084 / F62 / M-1914.
[5]	"Expression of AniA, the major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, provides protection against killing by normal human sera." Cardinale J.A., Clark V.L. Infect. Immun. 68:4368-4369(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTECTION AGAINST KILLING BY HUMAN SERA. Strain: ATCC 33084 / F62 / M-1914.
[6]	"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." Boulanger M.J., Murphy M.E.P. J. Mol. Biol. 315:1111-1127(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 42-364 IN COMPLEX WITH SUBSTRATE AND COPPER IONS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M97926 Genomic DNA. Translation: AAA25462.1.

PIR

A49208.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KBV	X-ray	1.95	A/B/C/D/E/F	42-364	[»]
1KBW	X-ray	2.40	A/B/C/D/E/F	42-364	[»]

ProteinModelPortal

Q02219.

SMR

Q02219. Positions 53-354.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.40.420. 2 hits.

InterPro

IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR001287. NO2-reductase_Cu.
[Graphical view]

Pfam

PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]

PRINTS

PR00695. CUNO2RDTASE.

SUPFAM

SSF49503. Cupredoxin. 2 hits.

TIGRFAMs

TIGR02376. Cu_nitrite_red. 1 hit.

PROSITE

PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q02219.

Entry information

Entry name

ANIA_NEIGO

Accession

Primary (citable) accession number: Q02219

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program