ID   ARCC2_STAAR             Reviewed;         313 AA.
AC   Q6GDH0;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Carbamate kinase 2;
DE            EC=2.7.2.2;
GN   Name=arcC2; OrderedLocusNames=SAR2711;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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=CAG41689.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX571856; CAG41689.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000660023.1; NC_002952.2.
DR   AlphaFoldDB; Q6GDH0; -.
DR   SMR; Q6GDH0; -.
DR   KEGG; sar:SAR2711; -.
DR   HOGENOM; CLU_076278_0_0_9; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00996; UER00366.
DR   Proteomes; UP000000596; 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..313
FT                   /note="Carbamate kinase 2"
FT                   /id="PRO_0000185135"
SQ   SEQUENCE   313 AA;  34293 MW;  D066A25828D09E99 CRC64;
     MKEKIVIALG GNAIQTKEAT AEAQQTAIRR AMQNLKPLFD SPARIVISHG NGPQIGGLLI
     QQAKSNSDTT PAMPLDTCGA MSQGMIGYWL ETEINRILTE MNSDRTVGTI VTRVEVDKDD
     PRFDNPTKPI GPFYTKEEVE ELQKEQPGSV FKEDAGRGYR KVVASPLPQS ILEHQLIRTL
     ADGKNIVIAC GGGGIPVIKK ENTYEGVEAV IDKDFASEKL ATLIEADTLM ILTNVENVFI
     NFNEPNQQQI DDIDVATLKK YAAQGKFAEG SMLPKIEAAI RFVESGENKK VIITNLEQAY
     EALIGNKGTH IHM