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Database: UniProt
Entry: A0A0W1QGY0_9SPHN
LinkDB: A0A0W1QGY0_9SPHN
Original site: A0A0W1QGY0_9SPHN 
ID   A0A0W1QGY0_9SPHN        Unreviewed;       357 AA.
AC   A0A0W1QGY0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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   ECO:0000313|EMBL:KTF67583.1};
GN   ORFNames=ATB93_02310 {ECO:0000313|EMBL:KTF67583.1};
OS   Sphingomonas sp. WG.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF67583.1, ECO:0000313|Proteomes:UP000052965};
RN   [1] {ECO:0000313|EMBL:KTF67583.1, ECO:0000313|Proteomes:UP000052965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WG {ECO:0000313|EMBL:KTF67583.1,
RC   ECO:0000313|Proteomes:UP000052965};
RA   Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.;
RT   "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing
RT   strain.";
RL   Submitted (NOV-2015) 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:KTF67583.1}.
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DR   EMBL; LNOS01000086; KTF67583.1; -; Genomic_DNA.
DR   RefSeq; WP_019368689.1; NZ_LNOS01000086.1.
DR   AlphaFoldDB; A0A0W1QGY0; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000052965; 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|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00038};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00038}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00038};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   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|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00038}; Reference proteome {ECO:0000313|Proteomes:UP000052965};
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        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        96..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        134..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        171..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        197..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        236..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        260..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        285..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        335..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   BINDING         189
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   357 AA;  38534 MW;  9BC02E31E7069E00 CRC64;
     MLYLIAEQLG FPGVLNLFRY LSFRTGGAVA TALLIGLLIG PKFIGWLRLR QGKGQPIRTD
     GPQSHLAKRG TPTMGGLMIL TSLTLALLIW MDLRNAYVWA CMFVTLGFGM IGFLDDYDKV
     RKQKTAGVSG KVRLIGEFLI AGVASAIIIF AEGNTQLYVP FLSWVHPDLG YFYIAFAAFT
     IVAFGNAVNL TDGLDGLATM PVVIAAMAFM LIAYLAGNKI YATYLGIPHV PGAGDLAIFC
     GAMIGAGLAF LWFNAPPAAV FMGDTGSLAL GGAIGTIAVT THHELVLGII GGLFVMEALS
     VIIQVFFFKR TGKRVFRMAP IHHHFEQLGW SEPTVVIRFW IIAFVLALAG LATLKLR
//
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