ID A0A2U8QV64_9FLAO Unreviewed; 405 AA.
AC A0A2U8QV64;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=DI487_09620 {ECO:0000313|EMBL:AWM14087.1};
OS Flavobacterium sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2201181 {ECO:0000313|EMBL:AWM14087.1, ECO:0000313|Proteomes:UP000245429};
RN [1] {ECO:0000313|EMBL:AWM14087.1, ECO:0000313|Proteomes:UP000245429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEBiC07310 {ECO:0000313|EMBL:AWM14087.1,
RC ECO:0000313|Proteomes:UP000245429};
RA Baek K.;
RT "Flavobacterium sp. MEBiC07310.";
RL Submitted (MAY-2018) 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}.
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DR EMBL; CP029463; AWM14087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8QV64; -.
DR KEGG; fse:DI487_09620; -.
DR OrthoDB; 9805475at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000245429; Chromosome.
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:UP000245429};
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 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 75..92
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 136..154
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 210..227
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 239..263
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 278..295
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 329..352
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 383..402
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 405 AA; 45145 MW; B195FB00AC410E9E CRC64;
MLYYLFQYLD KAFDVPGAGV FQYITFRSAM AFILSLAIAT IYGKKIINFL RKQQVGETIR
ELGLEGQTQK AGTPTMGGII IILATLVPVF LFARLENIYV ILLIITTLWM GTIGFIDDYI
KIFKKDKEGL KGRFKVIGQV GLGLIVGSVL YFHSGVTVRK DTMGARVKIE NVDTKFLQEK
STATTIPFLK NNEFDYAKVL SFMGDGYEKW AWLIFIPVVI FIITAVSNGA NLTDGIDGLA
AGTSAISVLT LGIFTFLSGN IIFSDYLNIM YIPNSGEMTI YIAAFVGALV GFLWYNTYPA
TVFMGDTGSL TIGGIIAVIA IAIRKELMIP ILCGIFLAEN LSVVLQVSYF KYTKKKYGEG
RRIFLMSPLH HHYQKKGYHE SKIVTRFWIV GILLAIFTLV SLKLR
//
