P09152 (NARG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Respiratory nitrate reductase 1 alpha chain
EC=1.7.99.4

Alternative name(s):
Nitrate reductase A subunit alpha
Quinol-nitrate oxidoreductase subunit alpha

Gene names

Name:	narG
Synonyms:	bisD, narC
Ordered Locus Names:	b1224, JW1215

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	1247 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	The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor.
Cofactor	Binds 1 4Fe-4S cluster per subunit. Binds 1 molybdenum ion per subunit. Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit.
Subunit structure	Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane. Interacts with the NarJ chaperone. Ref.13 Ref.14 Ref.15 Ref.16
Subcellular location	Cell membrane; Peripheral membrane protein.
Induction	By nitrate.
Domain	Apoenzyme contains at least 2 NarJ-binding sites, one interfering with membrane anchoring and another being involved in molybdenum insertion. The first binding-site is a short peptide sequence near the N-terminus that contains a twin-arginine homologous motif. Ref.14 Ref.15
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Cell membrane Membrane
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from expression pattern PubMed 7050087. Source: EcoCyc cytochrome complex assembly Inferred from direct assay Ref.11. Source: EcoCyc electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	intrinsic to membrane Inferred from direct assay PubMed 5996. Source: EcoCyc nitrate reductase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from direct assay Ref.18. Source: EcoCyc electron carrier activity Inferred from physical interaction PubMed 10504245. Source: EcoCyc molybdenum ion binding Inferred from direct assay Ref.18. Source: EcoCyc nitrate reductase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on NAD(P)H Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
narH	P11349	10	EBI-547248,EBI-555067
narJ	P0AF26	14	EBI-547248,EBI-555043
narW	P19317	3	EBI-547248,EBI-555088

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11

Chain

2 – 1247

1246

Respiratory nitrate reductase 1 alpha chain

PRO_0000063233

Sites

Metal binding

50

1

Iron-sulfur (4Fe-4S); via pros nitrogen

Metal binding

54

1

Iron-sulfur (4Fe-4S)

Metal binding

58

1

Iron-sulfur (4Fe-4S)

Metal binding

93

1

Iron-sulfur (4Fe-4S)

Metal binding

223

1

Molybdenum

Experimental info

Mutagenesis

50

1

H → S: Loss of activity. Ref.12

Sequence conflict

10

1

Y → K AA sequence Ref.11

Secondary structure

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1247

Helix Strand Turn

Details...

Helix

3 – 6

4

Helix

7 – 9

3

Helix

11 – 13

3

Beta strand

14 – 18

5

Turn

19 – 22

4

Beta strand

23 – 26

4

Helix

31 – 33

3

Helix

34 – 40

7

Beta strand

43 – 48

6

Beta strand

52 – 55

4

Beta strand

60 – 65

6

Beta strand

68 – 74

7

Helix

94 – 97

4

Helix

98 – 102

5

Beta strand

113 – 115

3

Helix

116 – 126

11

Helix

132 – 140

9

Helix

143 – 150

8

Turn

151 – 154

4

Beta strand

158 – 160

3

Helix

163 – 180

18

Helix

183 – 185

3

Beta strand

186 – 189

4

Helix

193 – 195

3

Helix

197 – 210

14

Beta strand

213 – 215

3

Turn

218 – 222

5

Helix

227 – 232

6

Helix

241 – 246

6

Beta strand

248 – 254

7

Helix

257 – 260

4

Helix

262 – 264

3

Helix

265 – 271

7

Helix

272 – 274

3

Beta strand

277 – 281

5

Helix

287 – 291

5

Beta strand

292 – 296

5

Turn

300 – 302

3

Helix

303 – 318

16

Turn

319 – 321

3

Helix

325 – 334

10

Beta strand

339 – 345

7

Beta strand

347 – 355

9

Helix

358 – 360

3

Beta strand

361 – 363

3

Helix

364 – 366

3

Helix

371 – 373

3

Beta strand

377 – 379

3

Helix

391 – 393

3

Beta strand

395 – 397

3

Beta strand

405 – 407

3

Turn

408 – 410

3

Turn

421 – 423

3

Beta strand

425 – 433

9

Beta strand

450 – 462

13

Beta strand

468 – 473

6

Helix

474 – 481

8

Beta strand

493 – 496

4

Helix

505 – 512

8

Helix

516 – 533

18

Beta strand

537 – 541

5

Helix

543 – 546

4

Helix

551 – 564

14

Beta strand

574 – 577

4

Helix

587 – 594

8

Turn

595 – 599

5

Beta strand

604 – 606

3

Helix

608 – 615

8

Helix

618 – 621

4

Helix

627 – 629

3

Helix

636 – 638

3

Helix

643 – 652

10

Beta strand

662 – 664

3

Turn

666 – 668

3

Helix

669 – 675

7

Helix

680 – 690

11

Beta strand

691 – 693

3

Helix

696 – 698

3

Beta strand

702 – 706

5

Beta strand

709 – 714

6

Turn

717 – 721

5

Beta strand

722 – 724

3

Helix

725 – 731

7

Turn

744 – 748

5

Beta strand

753 – 755

3

Beta strand

767 – 775

9

Helix

778 – 781

4

Beta strand

784 – 789

6

Beta strand

797 – 799

3

Beta strand

805 – 810

6

Beta strand

813 – 815

3

Helix

823 – 837

15

Turn

838 – 841

4

Beta strand

844 – 851

8

Helix

858 – 860

3

Beta strand

864 – 866

3

Helix

870 – 872

3

Turn

879 – 881

3

Beta strand

885 – 892

8

Helix

893 – 895

3

Helix

896 – 900

5

Helix

906 – 909

4

Beta strand

912 – 914

3

Beta strand

917 – 919

3

Helix

922 – 932

11

Beta strand

936 – 938

3

Turn

939 – 942

4

Beta strand

943 – 945

3

Helix

949 – 959

11

Turn

961 – 963

3

Helix

965 – 979

15

Helix

984 – 986

3

Helix

988 – 990

3

Helix

997 – 1002

6

Beta strand

1013 – 1015

3

Beta strand

1019 – 1021

3

Helix

1027 – 1032

6

Beta strand

1041 – 1043

3

Helix

1050 – 1054

5

Turn

1072 – 1078

7

Beta strand

1085 – 1090

6

Beta strand

1095 – 1098

4

Turn

1102 – 1104

3

Helix

1106 – 1111

6

Beta strand

1117 – 1121

5

Helix

1122 – 1128

7

Beta strand

1135 – 1140

6

Beta strand

1143 – 1152

10

Beta strand

1159 – 1161

3

Beta strand

1168 – 1171

4

Turn

1176 – 1178

3

Beta strand

1179 – 1181

3

Helix

1185 – 1187

3

Helix

1195 – 1197

3

Beta strand

1205 – 1207

3

Turn

1209 – 1211

3

Beta strand

1222 – 1227

6

Beta strand

1229 – 1231

3

Beta strand

1234 – 1238

5

Sequences

	Sequence		Length	Mass (Da)
	P09152 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 640ABAD5FF01DF25	FASTA	1,247	140,489
	10 20 30 40 50 60 MSKFLDRFRY FKQKGETFAD GHGQLLNTNR DWEDGYRQRW QHDKIVRSTH GVNCTGSCSW 70 80 90 100 110 120 KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPMMRKRLMK 130 140 150 160 170 180 MWREAKALHS DPVEAWASII EDADKAKSFK QARGRGGFVR SSWQEVNELI AASNVYTIKN 190 200 210 220 230 240 YGPDRVAGFS PIPAMSMVSY ASGARYLSLI GGTCLSFYDW YCDLPPASPQ TWGEQTDVPE 250 260 270 280 290 300 SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDLWLAPKQ 310 320 330 340 350 360 GTDAAMALAM GHVMLREFHL DNPSQYFTDY VRRYTDMPML VMLEERDGYY AAGRMLRAAD 370 380 390 400 410 420 LVDALGQENN PEWKTVAFNT NGEMVAPNGS IGFRWGEKGK WNLEQRDGKT GEETELQLSL 430 440 450 460 470 480 LGSQDEIAEV GFPYFGGDGT EHFNKVELEN VLLHKLPVKR LQLADGSTAL VTTVYDLTLA 490 500 510 520 530 540 NYGLERGLND VNCATSYDDV KAYTPAWAEQ ITGVSRSQII RIAREFADNA DKTHGRSMII 550 560 570 580 590 600 VGAGLNHWYH LDMNYRGLIN MLIFCGCVGQ SGGGWAHYVG QEKLRPQTGW QPLAFALDWQ 610 620 630 640 650 660 RPARHMNSTS YFYNHSSQWR YETVTAEELL SPMADKSRYT GHLIDFNVRA ERMGWLPSAP 670 680 690 700 710 720 QLGTNPLTIA GEAEKAGMNP VDYTVKSLKE GSIRFAAEQP ENGKNHPRNL FIWRSNLLGS 730 740 750 760 770 780 SGKGHEFMLK YLLGTEHGIQ GKDLGQQGGV KPEEVDWQDN GLEGKLDLVV TLDFRLSSTC 790 800 810 820 830 840 LYSDIILPTA TWYEKDDMNT SDMHPFIHPL SAAVDPAWEA KSDWEIYKAI AKKFSEVCVG 850 860 870 880 890 900 HLGKETDIVT LPIQHDSAAE LAQPLDVKDW KKGECDLIPG KTAPHIMVVE RDYPATYERF 910 920 930 940 950 960 TSIGPLMEKI GNGGKGIAWN TQSEMDLLRK LNYTKAEGPA KGQPMLNTAI DAAEMILTLA 970 980 990 1000 1010 1020 PETNGQVAVK AWAALSEFTG RDHTHLALNK EDEKIRFRDI QAQPRKIISS PTWSGLEDEH 1030 1040 1050 1060 1070 1080 VSYNAGYTNV HELIPWRTLS GRQQLYQDHQ WMRDFGESLL VYRPPIDTRS VKEVIGQKSN 1090 1100 1110 1120 1130 1140 GNQEKALNFL TPHQKWGIHS TYSDNLLMLT LGRGGPVVWL SEADAKDLGI ADNDWIEVFN 1150 1160 1170 1180 1190 1200 SNGALTARAV VSQRVPAGMT MMYHAQERIV NLPGSEITQQ RGGIHNSVTR ITPKPTHMIG 1210 1220 1230 1240 GYAHLAYGFN YYGTVGSNRD EFVVVRKMKN IDWLDGEGND QVQESVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer." Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V. Mol. Gen. Genet. 218:249-256(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / TG1.
[2]	"Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon." Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M. Mol. Gen. Genet. 222:104-111(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / TG1.
[3]	Blasco F. Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Strain: K12 / TG1.
[4]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Respiratory nitrate reductase of Escherichia coli. Sequence identification of the large subunit gene." McPherson M.J., Baron A.J., Pappin D.J.C., Wootton J.C. FEBS Lett. 177:260-264(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48. Strain: K12.
[8]	"Delineation of two distinct regulatory domains in the 5' region of the nar operon of Escherichia coli." Li S.F., Rabi T., Demoss J.A. J. Bacteriol. 164:25-32(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25. Strain: PK27.
[9]	"The narK gene product participates in nitrate transport induced in Escherichia coli nitrate-respiring cells." Noji S., Nohno T., Saito T., Taniguchi S. FEBS Lett. 252:139-143(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23. Strain: K12.
[10]	"Promoter region of the nar operon of Escherichia coli: nucleotide sequence and transcription initiation signals." Li S.F., Demoss J.A. J. Bacteriol. 169:4614-4620(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[11]	"Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli." Sodergren E.J., Hsu P.Y., Demoss J.A. J. Biol. Chem. 263:16156-16162(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11.
[12]	"Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit." Magalon A., Asso M., Guigliarelli B., Rothery R.A., Bertrand P., Giordano G., Blasco F. Biochemistry 37:7363-7370(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-50, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
[13]	"NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli." Blasco F., Dos Santos J.P., Magalon A., Frixon C., Guigliarelli B., Santini C.L., Giordano G. Mol. Microbiol. 28:435-447(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NARJ.
[14]	"Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli." Chan C.S., Howell J.M., Workentine M.L., Turner R.J. Biochem. Biophys. Res. Commun. 343:244-251(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NARJ, DOMAIN.
[15]	"NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly." Vergnes A., Pommier J., Toci R., Blasco F., Giordano G., Magalon A. J. Biol. Chem. 281:2170-2176(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NARJ, DOMAIN. Strain: K12 / MC4100 / JA176.
[16]	"Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase." Zakian S., Lafitte D., Vergnes A., Pimentel C., Sebban-Kreuzer C., Toci R., Claude J.B., Guerlesquin F., Magalon A. FEBS J. 277:1886-1895(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NARJ.
[17]	"Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A." Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J. Nat. Struct. Biol. 10:681-687(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[18]	"Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes." Jormakka M., Richardson D., Byrne B., Iwata S. Structure 12:95-104(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-1247.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16181 Genomic DNA. Translation: CAA34303.1.
X01164 Genomic DNA. Translation: CAA25611.1.
M11586 Genomic DNA. Translation: AAA24201.1.
U00096 Genomic DNA. Translation: AAC74308.1.
AP009048 Genomic DNA. Translation: BAA36094.1.
X15996 Genomic DNA. Translation: CAA34127.1.
L36649 Genomic DNA. Translation: AAA64296.1.

PIR

RDECNA. E64869.

RefSeq

NP_415742.1. NC_000913.2.
YP_489494.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q16	X-ray	1.90	A	1-1247	[»]
1R27	X-ray	2.00	A/C	2-1247	[»]
1SIW	X-ray	2.20	A	2-1246	[»]
1Y4Z	X-ray	2.00	A	2-1246	[»]
1Y5I	X-ray	1.90	A	2-1246	[»]
1Y5L	X-ray	2.50	A	2-1246	[»]
1Y5N	X-ray	2.50	A	2-1246	[»]
3EGW	X-ray	1.90	A	2-1245	[»]
3IR5	X-ray	2.30	A	1-1247	[»]
3IR6	X-ray	2.80	A	1-1247	[»]
3IR7	X-ray	2.50	A	1-1247	[»]

ProteinModelPortal

P09152.

SMR

P09152. Positions 2-1245.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10311N.

IntAct

P09152. 20 interactions.

MINT

MINT-1233973.

STRING

511145.b1224.

Protein family/group databases

TCDB

5.A.3.1.1. prokaryotic molybdopterin-containing oxidoreductase (PMO) family.

Proteomic databases

PaxDb

P09152.

PRIDE

P09152.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74308; AAC74308; b1224.
BAA36094; BAA36094; BAA36094.

GeneID

12934277.
945782.

KEGG

ecj:Y75_p1199.
eco:b1224.

PATRIC

32117708. VBIEscCol129921_1276.

Organism-specific databases

EchoBASE

EB0632.

EcoGene

EG10638. narG.

Phylogenomic databases

eggNOG

COG5013.

HOGENOM

HOG000237341.

KO

K00370.

OMA

NGIQGKD.

ProtClustDB

CLSK868288.

Enzyme and pathway databases

BioCyc

EcoCyc:NARG-MONOMER.
ECOL316407:JW1215-MONOMER.
MetaCyc:NARG-MONOMER.

Gene expression databases

Genevestigator

P09152.

Family and domain databases

Gene3D

2.40.40.20. 1 hit.

InterPro

IPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_Fe4S4_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR006468. NarG.
[Graphical view]

Pfam

PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]

SMART

SM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]

SUPFAM

SSF50692. Asp_decarb_fold. 1 hit.

TIGRFAMs

TIGR01580. narG. 1 hit.

PROSITE

PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

P09152.

Entry information

Entry name

NARG_ECOLI

Accession

Primary (citable) accession number: P09152
Secondary accession number(s): P78294

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 148 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program