ARCC1_STAAN
ID ARCC1_STAAN Reviewed; 310 AA.
AC Q7A627;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Carbamate kinase 1;
DE EC=2.7.2.2;
GN Name=arcC1; OrderedLocusNames=SA1013;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=N315;
RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT aureus during the post-exponential phase of growth.";
RL J. Microbiol. Methods 60:247-257(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42265.1; -; Genomic_DNA.
DR PIR; E89888; E89888.
DR RefSeq; WP_001074342.1; NC_002745.2.
DR AlphaFoldDB; Q7A627; -.
DR SMR; Q7A627; -.
DR SWISS-2DPAGE; Q7A627; -.
DR EnsemblBacteria; BAB42265; BAB42265; BAB42265.
DR KEGG; sau:SA1013; -.
DR HOGENOM; CLU_076278_0_0_9; -.
DR OMA; DWCGAQT; -.
DR UniPathway; UPA00996; UER00366.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
KW Arginine metabolism; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..310
FT /note="Carbamate kinase 1"
FT /id="PRO_0000269239"
SQ SEQUENCE 310 AA; 33596 MW; 04399CC277EB0BC7 CRC64;
MAKIVVALGG NALGKSPQEQ LELVKNTAKS LVGLITKGHE IVISHGNGPQ VGSINLGLNY
AAEHNQGPAF PFAECGAMSQ AYIGYQLQES LQNELHSIGM DKQVVTLVTQ VEVDENDPAF
NNPSKPIGLF YNKEEAEQIQ KEKGFIFVED AGRGYRRVVP SPQPISIIEL ESIKTLIKND
TLVIAAGGGG IPVIREQHDG FKGIDAVIDK DKTSALLGAN IQCDQLIILT AIDYVYINFN
TENQQPLKTT NVDELKRYID ENQFAKGSML PKIEAAISFI ENNPKGSVLI TSLNELDAAL
EGKVGTVIKK