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Database: UniProt
Entry: A0A2I0SJ61_9ACTN
LinkDB: A0A2I0SJ61_9ACTN
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ID   A0A2I0SJ61_9ACTN        Unreviewed;       356 AA.
AC   A0A2I0SJ61;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000256|HAMAP-Rule:MF_00038};
DE            EC=2.7.8.13 {ECO:0000256|HAMAP-Rule:MF_00038};
DE   AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00038};
GN   Name=mraY {ECO:0000256|HAMAP-Rule:MF_00038};
GN   ORFNames=CW362_26910 {ECO:0000313|EMBL:PKT69976.1};
OS   Streptomyces populi.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2058924 {ECO:0000313|EMBL:PKT69976.1, ECO:0000313|Proteomes:UP000236178};
RN   [1] {ECO:0000313|EMBL:PKT69976.1, ECO:0000313|Proteomes:UP000236178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A249 {ECO:0000313|EMBL:PKT69976.1,
RC   ECO:0000313|Proteomes:UP000236178};
RA   Wang Z.;
RT   "Streptomyces populusis sp. nov., a novel endophytic actinobacterium
RT   isolated from stems of Populus adenopoda Maxim.";
RL   Submitted (DEC-2017) 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:0000256|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:0000256|HAMAP-Rule:MF_00038};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00038,
CC         ECO:0000256|PIRSR:PIRSR600715-1};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00038}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00038};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00038}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC       subfamily. {ECO:0000256|ARBA:ARBA00005583, ECO:0000256|HAMAP-
CC       Rule:MF_00038}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKT69976.1}.
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DR   EMBL; PJOS01000061; PKT69976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0SJ61; -.
DR   OrthoDB; 9805475at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000236178; Unassembled WGS sequence.
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   NCBIfam; TIGR00445; mraY; 1.
DR   PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR   PANTHER; PTHR22926:SF5; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE HOMOLOG; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
DR   Pfam; PF10555; MraY_sig1; 1.
DR   PROSITE; PS01347; MRAY_1; 1.
DR   PROSITE; PS01348; MRAY_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00038, ECO:0000256|PIRSR:PIRSR600715-
KW   1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00038};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00038,
KW   ECO:0000256|PIRSR:PIRSR600715-1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236178};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00038};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00038};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00038}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        48..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        78..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        116..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        153..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        184..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        230..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        280..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        327..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         258
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   356 AA;  38237 MW;  24D279F620FCEE00 CRC64;
     MKQILFAGVL GLFLTLAGTP LLIKLLARKG YGQYIRDDGP REHASKRGTP TMGGIAFILA
     TIAAYFLSKL ITGYAPTYSG LLVLGLMFGM GLVGFLDDYI KIVKRRSLGL RAKAKMAGQL
     IVGIGFAVLA LMFPDNRGNT PASDKLSFIT DFGWKIGPVL FVLWALFMIL AMSNGVNLTD
     GLDGLATGAS VLVFGAYTFI GVWQFQESCA NATTLTNPGA CYEVRDPLDL AVVASALMGA
     CLGFLWWNTS PAKIFMGDTG SLALGGVLTG LAILSRTELL VAIMGGLFVL ITMSVVIQVG
     SFRLTGKRVF RMAPLQHHFE LKGWSEVLVV VRFWIIQGIC VIVGLGLFYA GWAAKK
//
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