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Urease subunit beta (EC 3.5.1.5) (Urea amidohydrolase subunit beta)

 A0A0G3DMT6_CAMLA        Unreviewed;       565 AA.
A0A0G3DMT6;
16-SEP-2015, integrated into UniProtKB/TrEMBL.
16-SEP-2015, sequence version 1.
10-OCT-2018, entry version 22.
RecName: Full=Urease subunit beta {ECO:0000256|HAMAP-Rule:MF_01953};
EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953};
AltName: Full=Urea amidohydrolase subunit beta {ECO:0000256|HAMAP-Rule:MF_01953};
Name=ureC {ECO:0000313|EMBL:AKJ52835.1};
Synonyms=ureB {ECO:0000256|HAMAP-Rule:MF_01953};
ORFNames=CD56_00035 {ECO:0000313|EMBL:AKJ52835.1};
Campylobacter lari.
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=201 {ECO:0000313|EMBL:AKJ52835.1, ECO:0000313|Proteomes:UP000035197};
[1] {ECO:0000313|Proteomes:UP000035197}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Slaughter Beach {ECO:0000313|Proteomes:UP000035197};
Meinersmann R.J., Lindsey R.L., Bono J.L., Loparev V.N.,
Genzlinger L.L., Oakley B.B.;
"Genome sequence of an urease-positive Campylobacter lari.";
Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: Urea + H(2)O = CO(2) + 2 NH(3).
{ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|RuleBase:RU000510,
ECO:0000256|SAAS:SAAS00354639}.
-!- COFACTOR:
Name=Ni cation; Xref=ChEBI:CHEBI:25516;
Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51,
ECO:0000256|RuleBase:RU000510};
Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51,
ECO:0000256|RuleBase:RU000510};
-!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
from urea (urease route): step 1/1. {ECO:0000256|HAMAP-
Rule:MF_01953, ECO:0000256|SAAS:SAAS00354661}.
-!- SUBUNIT: Heterohexamer of 3 UreA (alpha) and 3 UreB (beta)
subunits. {ECO:0000256|HAMAP-Rule:MF_01953}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PROSITE-ProRule:PRU00700,
ECO:0000256|SAAS:SAAS00548017}.
-!- PTM: Carbamylation allows a single lysine to coordinate two nickel
ions. {ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-50}.
-!- SIMILARITY: Belongs to the metallo-dependent hydrolases
superfamily. Urease alpha subunit family. {ECO:0000256|HAMAP-
Rule:MF_01953, ECO:0000256|RuleBase:RU004158,
ECO:0000256|SAAS:SAAS00849550}.
-!- CAUTION: The orthologous protein is known as the alpha subunit
(UreC) in most other bacteria. {ECO:0000256|HAMAP-Rule:MF_01953}.
-----------------------------------------------------------------------
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EMBL; CP011372; AKJ52835.1; -; Genomic_DNA.
RefSeq; WP_047207824.1; NZ_CP011372.1.
EnsemblBacteria; AKJ52835; AKJ52835; CD56_00035.
PATRIC; fig|201.18.peg.6; -.
UniPathway; UPA00258; UER00370.
Proteomes; UP000035197; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
CDD; cd00375; Urease_alpha; 1.
Gene3D; 2.30.40.10; -; 2.
HAMAP; MF_01953; Urease_alpha; 1.
InterPro; IPR006680; Amidohydro-rel.
InterPro; IPR011059; Metal-dep_hydrolase_composite.
InterPro; IPR032466; Metal_Hydrolase.
InterPro; IPR011612; Urease_alpha_N_dom.
InterPro; IPR017950; Urease_AS.
InterPro; IPR005848; Urease_asu.
InterPro; IPR017951; Urease_asu_c.
InterPro; IPR029754; Urease_Ni-bd.
PANTHER; PTHR43440; PTHR43440; 1.
Pfam; PF01979; Amidohydro_1; 1.
Pfam; PF00449; Urease_alpha; 1.
PRINTS; PR01752; UREASE.
SUPFAM; SSF51338; SSF51338; 1.
SUPFAM; SSF51556; SSF51556; 2.
TIGRFAMs; TIGR01792; urease_alph; 1.
PROSITE; PS01120; UREASE_1; 1.
PROSITE; PS00145; UREASE_2; 1.
PROSITE; PS51368; UREASE_3; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000035197};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
ProRule:PRU00700, ECO:0000256|SAAS:SAAS00432677};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
ProRule:PRU00700, ECO:0000256|RuleBase:RU000510,
ECO:0000256|SAAS:SAAS00444540};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
ECO:0000256|SAAS:SAAS00444531};
Nickel {ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
ECO:0000256|SAAS:SAAS00432700}.
DOMAIN 130 565 Urease. {ECO:0000259|PROSITE:PS51368}.
ACT_SITE 321 321 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-52,
ECO:0000256|PROSITE-ProRule:PRU00700}.
METAL 135 135 Nickel 1; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51}.
METAL 137 137 Nickel 1; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51}.
METAL 218 218 Nickel 1; via carbamate group.
{ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51}.
METAL 218 218 Nickel 2; via carbamate group.
{ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51}.
METAL 247 247 Nickel 2; via pros nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51}.
METAL 273 273 Nickel 2; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51}.
METAL 361 361 Nickel 1. {ECO:0000256|HAMAP-
Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-51}.
BINDING 220 220 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01953, ECO:0000256|PROSITE-
ProRule:PRU00700}.
MOD_RES 218 218 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_01953,
ECO:0000256|PIRSR:PIRSR611612-50}.
SEQUENCE 565 AA; 61443 MW; 4422FD53DBDBB623 CRC64;
MIKISKKDYV NMYGPTTNDR VRLADTDLIL RVEKDYTLYG EEVKFGGGKN IRDGMAQSVS
EGDFPDLVLT NALIVDYTGI YKADIGIKNG YIVGIGKAGN PDIQDGVDPS LIIGTSTDII
GAEGLIVTAG GIDTHIHFIS PTQIECALYS GVTTMIGGGI GPSEGTNATT CTSGAYHIHS
MLKATQNYPM NFGFLGKGNS SNKNALKEQI IAGACGLKIH EDWGATSSVI DASLNIADEM
DIQVAIHTDT LNEAGFVEDT IKAINGRVIH TFHTEGAGGG HAPDIIKMAG FKNVLPASTN
PTMPFTKNTI DEHLDMLMVC HHLDNKIKED VEFADSRIRP ETIAAEDKLH DMGVFSIMSS
DSQAMGRVGE VILRTWQSAD KCKKEFGALK EDNDLDDNFR IKRYIAKYTI NPAIAHGIDS
YVGSIEVGKF ADLVLWQPKF FGVKPKLILK GGLIVGAKIG DANASIPTPE PIIYEKMFGA
NLNENALHFV SKASLEANMP EKLSLKRKCV AVKNCRNITK KDLKFNDKVQ DIEVNPQTYE
VKINGELISS KSVDSLALAR KYFMI


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