ID N8ZU40_9GAMM Unreviewed; 101 AA.
AC N8ZU40;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Urease subunit beta {ECO:0000256|HAMAP-Rule:MF_01954};
DE EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01954};
DE AltName: Full=Urea amidohydrolase subunit beta {ECO:0000256|HAMAP-Rule:MF_01954};
GN Name=ureB {ECO:0000256|HAMAP-Rule:MF_01954};
GN ORFNames=F960_00566 {ECO:0000313|EMBL:ENV35268.1};
OS Acinetobacter gerneri DSM 14967 = CIP 107464 = MTCC 9824.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120926 {ECO:0000313|EMBL:ENV35268.1, ECO:0000313|Proteomes:UP000013117};
RN [1] {ECO:0000313|EMBL:ENV35268.1, ECO:0000313|Proteomes:UP000013117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107464 {ECO:0000313|EMBL:ENV35268.1,
RC ECO:0000313|Proteomes:UP000013117};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter gerneri CIP 107464.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000242, ECO:0000256|HAMAP-
CC Rule:MF_01954};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01954}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01954}.
CC -!- SIMILARITY: Belongs to the urease beta subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01954}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENV35268.1}.
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DR EMBL; APPN01000046; ENV35268.1; -; Genomic_DNA.
DR RefSeq; WP_004855243.1; NZ_KB849533.1.
DR AlphaFoldDB; N8ZU40; -.
DR STRING; 202952.GCA_000747725_03862; -.
DR GeneID; 84207982; -.
DR PATRIC; fig|1120926.3.peg.533; -.
DR eggNOG; COG0832; Bacteria.
DR HOGENOM; CLU_129707_1_1_6; -.
DR OrthoDB; 9797217at2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000013117; Unassembled WGS sequence.
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; Urease, beta subunit; 1.
DR HAMAP; MF_01954; Urease_beta; 1.
DR InterPro; IPR002019; Urease_beta-like.
DR InterPro; IPR036461; Urease_betasu_sf.
DR NCBIfam; TIGR00192; urease_beta; 1.
DR PANTHER; PTHR33569; UREASE; 1.
DR PANTHER; PTHR33569:SF1; UREASE; 1.
DR Pfam; PF00699; Urease_beta; 1.
DR SUPFAM; SSF51278; Urease, beta-subunit; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01954};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01954};
KW Reference proteome {ECO:0000313|Proteomes:UP000013117}.
SQ SEQUENCE 101 AA; 11058 MW; 5EA66242FF23C668 CRC64;
MIPGEIITPD ADIELNVGRQ TLKITVANLG DRPVQVGSHF HFYEANDALQ FDREAARGYR
LNIAAGTAIR FEPGQSRSIE LVALAGKREV YGFAGRVMGK L
//