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MRAY_CLOPE
ID   MRAY_CLOPE              Reviewed;         317 AA.
AC   Q8XJA1;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000255|HAMAP-Rule:MF_00038};
DE            EC=2.7.8.13 {ECO:0000255|HAMAP-Rule:MF_00038};
DE   AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038};
GN   Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038}; OrderedLocusNames=CPE1860;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
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   -!- FUNCTION: Catalyzes the initial step of the lipid cycle reactions in
CC       the biosynthesis of the cell wall peptidoglycan: transfers
CC       peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-
CC       pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding
CC       undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
CC       {ECO:0000255|HAMAP-Rule:MF_00038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC         D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-
CC         alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-
CC         alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-
CC         alanyl-D-alanine + UMP; Xref=Rhea:RHEA:28386, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:60392, ChEBI:CHEBI:61386, ChEBI:CHEBI:61387; EC=2.7.8.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00038};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00038};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00038}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00038};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00038}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}.
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DR   EMBL; BA000016; BAB81566.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8XJA1; -.
DR   SMR; Q8XJA1; -.
DR   STRING; 195102.gene:10491124; -.
DR   EnsemblBacteria; BAB81566; BAB81566; BAB81566.
DR   KEGG; cpe:CPE1860; -.
DR   HOGENOM; CLU_023982_0_1_9; -.
DR   OMA; LMSPLHH; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051992; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd06852; GT_MraY; 1.
DR   HAMAP; MF_00038; MraY; 1.
DR   InterPro; IPR000715; Glycosyl_transferase_4.
DR   InterPro; IPR003524; PNAcMuramoyl-5peptid_Trfase.
DR   InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR   PANTHER; PTHR22926; PTHR22926; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
DR   TIGRFAMs; TIGR00445; mraY; 1.
DR   PROSITE; PS01348; MRAY_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Magnesium; Membrane; Metal-binding;
KW   Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..317
FT                   /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT                   /id="PRO_0000108811"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        223..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
SQ   SEQUENCE   317 AA;  34502 MW;  797A1A82978FD936 CRC64;
     MIDPKIVMAI VISFIVASIL GPIIIPLLHK LKFGQNIRQE GPKSHLKKAG TPTIGGLIFI
     FATIITMFIM VGNPTDEAMI ALYSFVGFGF VGFLDDLLKI IKKKNEGLTS GQKMILLLIV
     SGFLTWYAYK YIGTSINIPF LNGQINFGLF YIPFVMFYFA GVTNAVNLTD GLDGLATSVT
     VLVTTFLGII SYNLGHISLA IFCVALAGAL LAFLRFNAFP ARVFMGDTGS LALGGAVAMV
     ALILKMPLIL VLIGIIYVIE TLSVILQVAS FKLTGKRIFK MAPIHHHFEQ LGWSETKIVS
     VFSIITVVFC FIAFASL
 
 
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