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MRAY_RHOPS
ID   MRAY_RHOPS              Reviewed;         361 AA.
AC   Q133W8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000255|HAMAP-Rule:MF_00038};
DE            EC=2.7.8.13 {ECO:0000255|HAMAP-Rule:MF_00038};
DE   AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038};
GN   Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038}; OrderedLocusNames=RPD_3397;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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:0000255|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:0000255|HAMAP-Rule:MF_00038};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00038};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00038}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00038}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}.
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DR   EMBL; CP000283; ABE40621.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q133W8; -.
DR   SMR; Q133W8; -.
DR   STRING; 316057.RPD_3397; -.
DR   EnsemblBacteria; ABE40621; ABE40621; RPD_3397.
DR   KEGG; rpd:RPD_3397; -.
DR   eggNOG; COG0472; Bacteria.
DR   HOGENOM; CLU_023982_0_0_5; -.
DR   OMA; LMSPLHH; -.
DR   OrthoDB; 1151822at2; -.
DR   BioCyc; RPAL316057:RPD_RS17085-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR22926; PTHR22926; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
DR   Pfam; PF10555; MraY_sig1; 1.
DR   TIGRFAMs; TIGR00445; mraY; 1.
DR   PROSITE; PS01347; MRAY_1; 1.
DR   PROSITE; PS01348; MRAY_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Magnesium; Membrane; Metal-binding;
KW   Peptidoglycan synthesis; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..361
FT                   /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT                   /id="PRO_1000003043"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
SQ   SEQUENCE   361 AA;  38560 MW;  716F8BDBB267764E CRC64;
     MLYWLIDLSS SIPAFNVFRY ITFRTGGAVV TGALFVFLCG PWIINNLRLR QGKGQPIRSD
     GPQSHLVTKK GTPTMGGLMI LSGLTVGTVL WANPVNPYVW IVLAVTLGFG FVGFYDDYMK
     VTKQTHAGIS GRTRLLIEFA IAGAACFALV WLGRSSLSSS LVIPFFKEVV LNLGWYFVIF
     GAFVIVGAGN AVNLTDGLDG LAIVPVMIAA ASFGLIAYLA GNAVFADYLQ INYVAGTGEL
     AVLCGALLGA GLGFLWFNAP PASIFMGDTG SLALGGMLGS IAVAVKHEIV LAVIGGLFVL
     EAVSVIVQVA SFKLTGKRVF RMAPIHHHFE QKGWTEPQIV IRFWIIAVML ALAGLATLKL
     R
 
 
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