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Database: UniProt
Entry: L1N0Z3_9BACT
LinkDB: L1N0Z3_9BACT
Original site: L1N0Z3_9BACT 
ID   L1N0Z3_9BACT            Unreviewed;       423 AA.
AC   L1N0Z3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=HMPREF9151_02354 {ECO:0000313|EMBL:EKX96871.1};
OS   Hoylesella saccharolytica F0055.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hoylesella.
OX   NCBI_TaxID=1127699 {ECO:0000313|EMBL:EKX96871.1, ECO:0000313|Proteomes:UP000010433};
RN   [1] {ECO:0000313|EMBL:EKX96871.1, ECO:0000313|Proteomes:UP000010433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0055 {ECO:0000313|EMBL:EKX96871.1,
RC   ECO:0000313|Proteomes:UP000010433};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) 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:EKX96871.1}.
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DR   EMBL; AMEP01000150; EKX96871.1; -; Genomic_DNA.
DR   RefSeq; WP_009161214.1; NZ_KB290963.1.
DR   AlphaFoldDB; L1N0Z3; -.
DR   STRING; 1127699.HMPREF9151_02354; -.
DR   PATRIC; fig|1127699.3.peg.2153; -.
DR   HOGENOM; CLU_023982_0_0_10; -.
DR   OrthoDB; 9805475at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000010433; 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   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:UP000010433};
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        71..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..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        211..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        241..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        280..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        304..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        331..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        401..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   423 AA;  47412 MW;  D34026464818DDFE CRC64;
     MLYYLFRFLE QYGISGAHIW GYISFRSLLA MIFSLVISAW FGEKFIKYLK SKQITEVQRD
     VAIDPFGVNK IGVPSMGGVI IIVAILIPVL LLGRLRNTYL ILMVITTVWL GFLGGMDDFI
     KIFRHNKEGL KGKYKIVGQV GIGLIVGLVL WASPDVKINE NLAVEHQNGT EMVVRHRTEA
     RKSLKTTIPF VKGHNLDYSH ITAFMGKYKT AAGWILFVIM TIIVVTAVSN GANLNDGMDG
     MCAGNSAIIG VVLGILAYVS SHIEFASYLN IMYIPGSQEL VVFFCAFIGA LIGFLWYNAY
     PAQVFMGDTG SLTIGGIIAV GAIIIHKELL LPILCGIFFI ESLSVILQVW YYKMGKRRGI
     KQRIFRRTPI HDNFRTQDHQ LDPECTYVFK KSKGTVHESK ITIRFWIITI ILAALTIITL
     KIR
//
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