ID   ARCC_STAEQ              Reviewed;         310 AA.
AC   Q5HKJ3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Carbamate kinase;
DE            EC=2.7.2.2;
GN   Name=arcC; OrderedLocusNames=SERP2352;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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}.
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DR   EMBL; CP000029; AAW53149.1; -; Genomic_DNA.
DR   RefSeq; WP_001830533.1; NC_002976.3.
DR   AlphaFoldDB; Q5HKJ3; -.
DR   SMR; Q5HKJ3; -.
DR   STRING; 176279.SERP2352; -.
DR   EnsemblBacteria; AAW53149; AAW53149; SERP2352.
DR   GeneID; 50017624; -.
DR   KEGG; ser:SERP2352; -.
DR   eggNOG; COG0549; Bacteria.
DR   HOGENOM; CLU_076278_0_0_9; -.
DR   OMA; DWCGAQT; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00996; UER00366.
DR   Proteomes; UP000000531; 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   Reference proteome; Transferase.
FT   CHAIN           1..310
FT                   /note="Carbamate kinase"
FT                   /id="PRO_0000185140"
SQ   SEQUENCE   310 AA;  33546 MW;  404BC2ACC0857076 CRC64;
     MAKIVVALGG NALGKSPQEQ LELVKNTAKS LVGLITKGHE IVISHGNGPQ VGSINLGLNY
     AAEHDQGPAF PFAECGAMSQ AYIGYQLQES LQNELHSMGI DKQVVTLVTQ VEVDEGDPAF
     NSPSKPIGLF YTKEEANRIQ QEKGYQFVED AGRGYRRVVP SPQPISIIEL ESIKTLVEND
     TLVIAAGGGG IPVIREQHDS FKGIDAVIDK DKTSALLGAD IHCDQLIILT AIDYVYINYH
     TDQQQALKTT NIDTLKTYIE EEQFAKGSML PKIESAISFI ENNPNGSVLI TSLNQLDAAL
     EGKIGTLITK