Reviewed, UniProtKB/Swiss-Prot O86508 (URE12_STRCO)

Names and origin

Protein names

Recommended name:
    Urease subunit alpha 2
    EC=3.5.1.5
Alternative name(s):
    Urea amidohydrolase subunit alpha 2

Gene names

Name:	ureC2
Ordered Locus Names:	SCO5526
ORF Names:	SC1C2.07

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953
Cofactor	Binds 2 nickel ions per subunit By similarity.
Pathway	Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP MF_01953
Subunit structure	May form a heterohexamer of 3 ureC (alpha) and 3 ureAB (gamma/beta) subunits. May also form a heterotrimer of ureA (gamma), ureB (beta) and ureC (alpha) subunits. Three heterotrimers associate to form the active enzyme By similarity.
Subcellular location	Cytoplasm By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two nickel ions By similarity.
Sequence similarities	Belongs to the urease family. Contains 1 urease domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Nickel
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	urea metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW urease activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 558	558	Urease subunit alpha 2 HAMAP MF_01953		PRO_0000234188
Regions
	Domain	129 – 558	430	Urease
Sites
	Active site	317	1	Proton donor By similarity
	Metal binding	134	1	Nickel 2 By similarity
	Metal binding	136	1	Nickel 2 By similarity
	Metal binding	214	1	Nickel 1; via carbamate group By similarity
	Metal binding	214	1	Nickel 2; via carbamate group By similarity
	Metal binding	243	1	Nickel 1 By similarity
	Metal binding	269	1	Nickel 1 By similarity
	Metal binding	357	1	Nickel 2 By similarity
	Binding site	216	1	Substrate By similarity
Amino acid modifications
	Modified residue	214	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O86508-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 77C046B360256324	FASTA	558	58,351
	10 20 30 40 50 60 MTIDPYAYAA AHGPRAGDRL RLGDSGLVIR VESDAQHYGD EFLAGFGKTA RDGLHLKAAA 70 80 90 100 110 120 VRDTCDVVIS NVVVIDAVQG IRKVSIGIRE GRVHAIGRAG NPDTLDGVDV VVGTGTSIVS 130 140 150 160 170 180 GEGLIATAGA VDTHVHLLSP RIMEASLASG VTTIIGQEFG PVWGVGVNSP WALKHAFGAF 190 200 210 220 230 240 DAWPVNIGFL GRGSSSHEAP LIEALAEGGA SGFKVHEDMG AHTRALDTAL RVAEEHDVQV 250 260 270 280 290 300 ALHSDGLNEC LSVEDTLRVL DGRTIHAFHI EGCGGGHVPN VLKMAGVPHV IGSSTNPTLP 310 320 330 340 350 360 FGRDAVAEHY GMIVSVHDLK TDLPGDAAMA RDRIRAGTMG AEDVLHDLGA IGITSSDAQG 370 380 390 400 410 420 MGRAGETVRR TFAMAGKMKA QFGAEGDDDN ARVLRYIAKL TINPALAHGL AHEVGSIEVG 430 440 450 460 470 480 KLADLVLWRP DHFGAKPQLV LKSGFPAYGV VGDPNAATDT CEPLVLGPQF GAHGATPAEI 490 500 510 520 530 540 SVAFVAQAAL DQGGDTMPTR RRRVAVRGTR GIGPADLRLN SRTGAVDVDQ RTGLVTLDGD 550 PLRSEPAESV SLNRLYFL

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL939124 Genomic DNA. Translation: CAA19974.1.
PIR	T29056.
RefSeq	NP_629660.1.
3D structure databases
HSSP	HSSP built from PDB template 1EJX based on UniProtKB P18314.
ModBase	Search...
Genome annotation databases
GeneID	1100966.
GenomeReviews	Gene locus SCO5526 in contig AL645882_GR.
KEGG	sco:SCO5526.
NMPDR	fig|100226.1.peg.5478.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O86508.
OMA	GKTARDG.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO5526-MON.
BRENDA	3.5.1.5. 1084.
Family and domain databases
HAMAP	MF_01953. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR011612. Urease_alpha_N. IPR017951. Urease_asu_c. IPR017952. Urease_asu_core. IPR017950. Urease_asu_CS. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. PF00449. Urease_alpha. 1 hit. [Graphical view]
PRINTS	PR01752. UREASE.
PROSITE	PS01120. UREASE_1. 1 hit. PS00145. UREASE_2. False negative. PS51368. UREASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

URE12_STRCO

Accession

Primary (citable) accession number: O86508

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	November 1, 1998
Last modified:	November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)