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MRAY_ACTP7
ID   MRAY_ACTP7              Reviewed;         360 AA.
AC   B3GZK5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=APP7_0015;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) 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; CP001091; ACE60667.1; -; Genomic_DNA.
DR   RefSeq; WP_012478273.1; NC_010939.1.
DR   AlphaFoldDB; B3GZK5; -.
DR   SMR; B3GZK5; -.
DR   EnsemblBacteria; ACE60667; ACE60667; APP7_0015.
DR   KEGG; apa:APP7_0015; -.
DR   HOGENOM; CLU_023982_0_0_6; -.
DR   OMA; LMSPLHH; -.
DR   BioCyc; APLE537457:APP7_RS00075-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001226; 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..360
FT                   /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT                   /id="PRO_1000090584"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        288..308
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   360 AA;  40087 MW;  153559646FBE8728 CRC64;
     MLVWLAEYLV QYNTAFNVVS YITFRAIMAL LTAMGIGLWI GPEVIRRLQL LKFGQEVRND
     GPESHFKKRG TPTMGGIMIL IAIGVSTLLW ADLRNSYVWF VLFVLFGYGA VGFVDDYWKI
     KRKNTDGLIA RWKYFWLSVI ALIAVFGIYA VGKDTAATQL VVPFFKEFMP QLGIFFIILS
     YFVIVGTSNA VNLTDGLDGL AIVPTIMVAS AFALIAWATG NFNFAQYLHI PFVPNAGELV
     ILCTAIVGAG LGFLWYNTYP AQVFMGDVGS LSLGGALGTI AVLVRQELLL VIMGGVFVVE
     ALSVILQVGS YKLRQKRIFR MAPIHHHFEL KGWPEPRVIV CFWIITLMLV LIGLVTLKLR
 
 
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