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CDSA_MYCTU
ID   CDSA_MYCTU              Reviewed;         328 AA.
AC   P9WPF7; L0TDN0; P63758; Q10807;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 2.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Phosphatidate cytidylyltransferase;
DE            EC=2.7.7.41;
DE   AltName: Full=CDP-DAG synthase;
DE   AltName: Full=CDP-DG synthase;
DE   AltName: Full=CDP-diacylglycerol synthase;
DE            Short=CDS;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase;
DE   AltName: Full=CDP-diglyceride synthase;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase;
GN   Name=cdsA; OrderedLocusNames=Rv2881c; ORFNames=MTCY274.12c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-39, AND SEQUENCE REVISION TO N-TERMINUS.
RC   STRAIN=H37Rv;
RX   PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA   Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA   Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT   "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT   annotated encoding genes.";
RL   Genomics 114:292-304(2022).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 (ISOFORM 2), CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC         diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=P9WPF7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P9WPF7-2; Sequence=VSP_059173, VSP_059174;
CC   -!- MISCELLANEOUS: [Isoform 2]: Starts at GUG codon. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCP45683.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:21969609, ECO:0000269|PubMed:34915127};
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DR   EMBL; AL123456; CCP45683.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70924; D70924.
DR   RefSeq; NP_217397.1; NC_000962.3. [P9WPF7-2]
DR   AlphaFoldDB; P9WPF7; -.
DR   SMR; P9WPF7; -.
DR   STRING; 83332.Rv2881c; -.
DR   PaxDb; P9WPF7; -.
DR   DNASU; 888910; -.
DR   GeneID; 888910; -.
DR   KEGG; mtu:Rv2881c; -.
DR   TubercuList; Rv2881c; -.
DR   eggNOG; COG4589; Bacteria.
DR   OMA; FGKHPMA; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR000374; PC_trans.
DR   PROSITE; PS01315; CDS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative initiation; Cell membrane;
KW   Direct protein sequencing; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..328
FT                   /note="Phosphatidate cytidylyltransferase"
FT                   /id="PRO_0000090743"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          15..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..22
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_059173"
FT   VAR_SEQ         23
FT                   /note="V -> M (in isoform 2)"
FT                   /id="VSP_059174"
FT   INIT_MET        P9WPF7-2:1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   MOD_RES         P9WPF7-2:2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
SQ   SEQUENCE   328 AA;  34458 MW;  3C80533E32CD2ED1 CRC64;
     MSWLNTKKAS CWRSSGRSAT KSVTTNDAGT GNPAEQPARG AKQQPATETS RAGRDLRAAI
     VVGLSIGLVL IAVLVFVPRV WVAIVAVATL VATHEVVRRL REAGYLIPVI PLLIGGQAAV
     WLTWPFGAVG ALAGFGGMVV VCMIWRLFMQ DSVTRPTTGG APSPGNYLSD VSATVFLAVW
     VPLFCSFGAM LVYPENGSGW VFCMMIAVIA SDVGGYAVGV LFGKHPMVPT ISPKKSWEGF
     AGSLVCGITA TIITATFLVG KTPWIGALLG VLFVLTTALG DLVESQVKRD LGIKDMGRLL
     PGHGGLMDRL DGILPSAVAA WIVLTLLP
 
 
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