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Database: UniProt
Entry: A0A066WU60_9FLAO
LinkDB: A0A066WU60_9FLAO
Original site: A0A066WU60_9FLAO 
ID   A0A066WU60_9FLAO        Unreviewed;       409 AA.
AC   A0A066WU60;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=FEM21_24610 {ECO:0000313|EMBL:KDN54499.1};
OS   Flavobacterium seoulense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1492738 {ECO:0000313|EMBL:KDN54499.1, ECO:0000313|Proteomes:UP000027064};
RN   [1] {ECO:0000313|EMBL:KDN54499.1, ECO:0000313|Proteomes:UP000027064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1321 {ECO:0000313|EMBL:KDN54499.1,
RC   ECO:0000313|Proteomes:UP000027064};
RA   Shin S.-K., Yi H.;
RT   "Genome Sequence of Flavobacterium sp. EM1321.";
RL   Submitted (MAY-2014) 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:KDN54499.1}.
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DR   EMBL; JNCA01000022; KDN54499.1; -; Genomic_DNA.
DR   RefSeq; WP_035660673.1; NZ_JNCA01000022.1.
DR   AlphaFoldDB; A0A066WU60; -.
DR   STRING; 1492738.FEM21_24610; -.
DR   PATRIC; fig|1492738.3.peg.2448; -.
DR   eggNOG; COG0472; Bacteria.
DR   OrthoDB; 9805475at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000027064; 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   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..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        99..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        214..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        243..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        282..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        306..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        333..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        387..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   409 AA;  45541 MW;  EF6DB55841861F57 CRC64;
     MLYYLFDYLN KTLNISGTGV FQYITFRSSL AFILSLLLST IYGKRVISFL QRQQVGETIR
     ELGLKGQNEK AGTPTMGGLI IIFATLIPVF LFAKLHNIYV VLLIVTTLWM GTIGFVDDYI
     KIFKKDKEGL KGIFKVFGQV GLGLIVGCVL YFNPQVTVRT DTGKIDVFRQ TTETVVVPAG
     IEEKSTATTI PFFKNNEFDY AEVLAWTGDG YEKWAWLIYI PVVIFIITAV SNGANLTDGI
     DGLAAGTSAI SVLALAIFTF VSGNIIFSNY LNIMYIPNSG EMTVFIAAFV GALIGFLWYN
     SYPASVFMGD TGSLTIGGII AVLAIAVRKE LLIPLLCGIF LVENFSVVLQ VSYFKYTKKR
     FGEGRRIFLM SPLHHHYQKK GYHESKIVTR FWIVAILLAI LSIVTLKLR
//
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