ID   URE2_ALCBS              Reviewed;         101 AA.
AC   Q0VKY0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Urease subunit beta {ECO:0000255|HAMAP-Rule:MF_01954};
DE            EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01954};
DE   AltName: Full=Urea amidohydrolase subunit beta {ECO:0000255|HAMAP-Rule:MF_01954};
GN   Name=ureB {ECO:0000255|HAMAP-Rule:MF_01954}; OrderedLocusNames=ABO_2720;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01954};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01954}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC       subunits. Three heterotrimers associate to form the active enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_01954}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01954}.
CC   -!- SIMILARITY: Belongs to the urease beta subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01954}.
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DR   EMBL; AM286690; CAL18168.1; -; Genomic_DNA.
DR   RefSeq; WP_011589991.1; NC_008260.1.
DR   AlphaFoldDB; Q0VKY0; -.
DR   SMR; Q0VKY0; -.
DR   STRING; 393595.ABO_2720; -.
DR   EnsemblBacteria; CAL18168; CAL18168; ABO_2720.
DR   KEGG; abo:ABO_2720; -.
DR   eggNOG; COG0832; Bacteria.
DR   HOGENOM; CLU_129707_1_1_6; -.
DR   OMA; FYEVNDA; -.
DR   OrthoDB; 1755809at2; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000008871; Chromosome.
DR   GO; GO:0035550; C:urease complex; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00407; Urease_beta; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   HAMAP; MF_01954; Urease_beta; 1.
DR   InterPro; IPR002019; Urease_beta.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   Pfam; PF00699; Urease_beta; 1.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..101
FT                   /note="Urease subunit beta"
FT                   /id="PRO_1000070711"
SQ   SEQUENCE   101 AA;  11179 MW;  E5F71B61B8A7B405 CRC64;
     MIPGEYAIQN GDIEINPGRE TLSVEVANTG DRPIQVGSHY HFYEANNALQ FDREKTRGFR
     LNIPAGTAVR IEPGQSRTVE LVAYAGQRKV YGFQGKVMGP L