ARCC_STAHJ
ID ARCC_STAHJ Reviewed; 309 AA.
AC Q4L9V7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Carbamate kinase;
DE EC=2.7.2.2;
GN Name=arcC; OrderedLocusNames=SH0259;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate +
CC H(+) + H2O; Xref=Rhea:RHEA:10152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=2.7.2.2;
CC -!- PATHWAY: Metabolic intermediate metabolism; carbamoyl phosphate
CC degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE03568.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP006716; BAE03568.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011274588.1; NC_007168.1.
DR AlphaFoldDB; Q4L9V7; -.
DR SMR; Q4L9V7; -.
DR STRING; 279808.SH0259; -.
DR EnsemblBacteria; BAE03568; BAE03568; SH0259.
DR KEGG; sha:SH0259; -.
DR eggNOG; COG0549; Bacteria.
DR HOGENOM; CLU_076278_0_0_9; -.
DR OrthoDB; 901370at2; -.
DR UniPathway; UPA00996; UER00366.
DR Proteomes; UP000000543; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008804; F:carbamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035975; P:carbamoyl phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04235; AAK_CK; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR003964; Carb_kinase.
DR PANTHER; PTHR30409; PTHR30409; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000723; Carbamate_kin; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR00746; arcC; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..309
FT /note="Carbamate kinase"
FT /id="PRO_0000269245"
SQ SEQUENCE 309 AA; 33127 MW; B85DAAFC53D93149 CRC64;
MSKIVVALGG NALGQSPEEQ LELVKGTAKS LVSLIQKGYE VVISHGNGPQ VGSINLGLNY
AAENGQGPAF PFPECGAMSQ AYIGYQLQES LLNELHVLNI DKQVVTLVTQ VEVAGDDQAF
NNPTKPIGLF YTKEQAEQTM EEKGYKFVED SGRGYRRVVP SPMPINIVEL DSIETLIKHG
TLVIAAGGGG IPVVKEEGNY KGVDAVIDKD KTSALLAAHL KSDQLIILTA VDYVYINYGK
DNQEALGEVT VDEMNQHIAD GQFAKGSMLP KVEAALQFIE KNPEGSVLIT SLEDLGDALD
GKIGTLIKK