ID A0A239XLV8_9FLAO Unreviewed; 413 AA.
AC A0A239XLV8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:SNV47113.1};
GN ORFNames=SAMEA4412677_01682 {ECO:0000313|EMBL:SNV47113.1};
OS Chryseobacterium taklimakanense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=536441 {ECO:0000313|EMBL:SNV47113.1, ECO:0000313|Proteomes:UP000215196};
RN [1] {ECO:0000313|EMBL:SNV47113.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13490 {ECO:0000313|EMBL:SNV47113.1};
RG Pathogen Informatics;
RL Submitted (JUN-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 ---------------------------------------------------------------------------
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; LT906465; SNV47113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239XLV8; -.
DR KEGG; ctak:4412677_01682; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000215196; Chromosome 1.
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:UP000215196};
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 25..44
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 76..93
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 99..117
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 137..154
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..262
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..354
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 391..410
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 413 AA; 46210 MW; C4C7F4CA3BB9E32B CRC64;
MLYYLYEYLT ANGIHIPGLN LLRYISFRAA ISVLMSLAIA LIYGKKIINF LRRRQMGELV
RDLGLEGQKQ KEGTPTMGGL IIILATIIPV LLFTKVLNVY ILLLLISVVW MGAIGFIDDY
LKKIKKNKDG LSGKFKVIGQ VGLGLIVGVT MYFHPDVVVK RKYADAQVVN RNNVEQNFME
TEKATVSTVP FVKNNEFDYS GVLFWMDADE RHENAWMVFI PLVIFIVTAV SNGANITDGI
DGLAAGTSAV ILLTLAFFAY VSGNIIFADY LNIMFLPNMG ETTIFAVAMV GAVIGFFWYN
TYPAQVFMGD TGSLMLGGVI AVLAIILRKE LLIPVLCGIF LIENISVMLQ VGVFKYRKRK
FGLEYAQANR LFKMSPLHHH YQKSGYHESK IVNRMIIIGV MLAIICLITL KVR
//
