位置:首页 > 蛋白库 > MRAY_BURM1
MRAY_BURM1
ID   MRAY_BURM1              Reviewed;         389 AA.
AC   A9AJ19;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 90.
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};
GN   OrderedLocusNames=Bmul_2839, BMULJ_00399;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00038}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000868; ABX16523.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG42367.1; -; Genomic_DNA.
DR   RefSeq; WP_006400444.1; NC_010804.1.
DR   AlphaFoldDB; A9AJ19; -.
DR   SMR; A9AJ19; -.
DR   STRING; 395019.Bmul_2839; -.
DR   EnsemblBacteria; BAG42367; BAG42367; BMULJ_00399.
DR   GeneID; 66525375; -.
DR   KEGG; bmj:BMULJ_00399; -.
DR   KEGG; bmu:Bmul_2839; -.
DR   eggNOG; COG0472; Bacteria.
DR   HOGENOM; CLU_023982_0_0_4; -.
DR   OMA; LMSPLHH; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008815; Chromosome 1.
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   Pfam; PF10555; MraY_sig1; 1.
DR   TIGRFAMs; TIGR00445; mraY; 1.
DR   PROSITE; PS01347; MRAY_1; 1.
DR   PROSITE; PS01348; MRAY_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell inner membrane; 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..389
FT                   /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT                   /id="PRO_1000090602"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
SQ   SEQUENCE   389 AA;  42841 MW;  6831AC3E4350673B CRC64;
     MLLALAQWLQ GDASFLRLFT YLTFRAVMAT ITALGIGLVC GPWVIRKLTE MKVGQAVRKD
     GPQTHLVKSG TPTMGGVLIL IGIAVATLLW GDLTNRFIWI VMLVTFGFGV IGWVDDYRKV
     VYKDPRGMSS REKYFWQSVI GLFAAVYLAF SVSEANNVRV FDLFMAWVRS GLSMGLPARA
     DLMLPFLKSI SYPLGVWGFI ALTYFVIVGA SNAVNLTDGL DGLVIMPVVL VGASLGVFAY
     VMGSAVYSKY LLFPHIPGAG ELLIFCSAMG GAGLAFLWYN THPAQVFMGD VGALALGGAL
     GTVAVIVRQE IVLFIMGGIF VAETLSVMLQ VTWFKYTKKR YGEGRRIFKM APLHHHFELS
     GWKETQVVVR FWIITLMLCL FGLSTLKLR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024