ID   ARCC_ECOL6              Reviewed;         297 AA.
AC   Q8FK51;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Carbamate kinase;
DE            EC=2.7.2.2;
GN   Name=arcC; OrderedLocusNames=c0635;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN79112.1; -; Genomic_DNA.
DR   RefSeq; WP_000855367.1; NC_004431.1.
DR   AlphaFoldDB; Q8FK51; -.
DR   SMR; Q8FK51; -.
DR   STRING; 199310.c0635; -.
DR   EnsemblBacteria; AAN79112; AAN79112; c0635.
DR   KEGG; ecc:c0635; -.
DR   eggNOG; COG0549; Bacteria.
DR   HOGENOM; CLU_076278_0_1_6; -.
DR   OMA; ESQGFIG; -.
DR   BioCyc; ECOL199310:C0635-MON; -.
DR   UniPathway; UPA00996; UER00366.
DR   Proteomes; UP000001410; 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..297
FT                   /note="Carbamate kinase"
FT                   /id="PRO_0000185120"
SQ   SEQUENCE   297 AA;  31742 MW;  664317C6060A9649 CRC64;
     MKTLVVALGG NALLQRGEAL TAENQYRNIA SAVPALARLA RSYRLAIVHG NGPQVGLLAL
     QNLAWKEVEP YPLDVLVAES QGMIGYMLAQ SLSAQPQMPH VTTVLTRIEV SPDDPAFLQP
     EKFIGPVYQP EEQEALEATY GWQMKRDGKY LRRVVASPQP RKILDSEAIE LLLKEGHVVI
     CSGGGGVPVT EDGAGSEAVI DKDLAAALLA EQINADGLVI LTDADAVYEN WGTPQQRAIR
     HATPDELAPF AKADGSMGPK VTAVSGYVRS RGKPAWIGAL SRIEETLAGE AGTCISL