ID   ARCC_CLOPE              Reviewed;         314 AA.
AC   Q46171;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Carbamate kinase;
DE            EC=2.7.2.2;
GN   Name=arcC; OrderedLocusNames=CPE0171;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=9053381; DOI=10.1111/j.1574-6968.1997.tb10186.x;
RA   Ohtani K., Bando M., Swe T., Banu S., Oe M., Hayashi H., Shimizu T.;
RT   "Collagenase gene (colA) is located in the 3'-flanking region of the
RT   perfringolysin O (pfoA) locus in Clostridium perfringens.";
RL   FEMS Microbiol. Lett. 146:155-159(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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; X97768; CAA66367.1; -; Genomic_DNA.
DR   EMBL; BA000016; BAB79877.1; -; Genomic_DNA.
DR   RefSeq; WP_003462795.1; NC_003366.1.
DR   AlphaFoldDB; Q46171; -.
DR   SMR; Q46171; -.
DR   STRING; 195102.gene:10489415; -.
DR   EnsemblBacteria; BAB79877; BAB79877; BAB79877.
DR   GeneID; 29572714; -.
DR   KEGG; cpe:CPE0171; -.
DR   HOGENOM; CLU_076278_0_0_9; -.
DR   OMA; DWCGAQT; -.
DR   UniPathway; UPA00996; UER00366.
DR   Proteomes; UP000000818; 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..314
FT                   /note="Carbamate kinase"
FT                   /id="PRO_0000185118"
FT   CONFLICT        9
FT                   /note="G -> E (in Ref. 1; CAA66367)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="K -> T (in Ref. 1; CAA66367)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  33864 MW;  170C59630EBD1A37 CRC64;
     MKIVLALGGN ALQKDSKDKS AEGQLETCRQ TAISVADLIE DGHEVSIVHG NGPQVGQILA
     SIELAHQVDN GNPLFPFDVV GAFSEGYIGY HLQNTIREEL LKRGIEKSVD TITTQVIVDK
     NDPGFKNPTK PIGSFYTKEE AEKLEKDKGY TMKEDAGRGY RRVVASPKPV DIVEKEAIKT
     MVDSGFIVIA CGGGGIPVVE DGDRLEGVPA VIDKDFAAEK LAEILDADAL LILTAVDRVC
     VNFNKPDQKA LKEINLEEVD KYIEEGQFAP GSMLPKVEAC KKFVLSGDKK VAIIASLTNA
     KAALRGESGT KIVK