MRAY_BEUC1
ID MRAY_BEUC1 Reviewed; 360 AA.
AC C5BW62;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=Bcav_2413;
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinobacteria; Micrococcales; Beutenbergiaceae; Beutenbergia.
OX NCBI_TaxID=471853;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432;
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00038};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP001618; ACQ80663.1; -; Genomic_DNA.
DR RefSeq; WP_015882903.1; NC_012669.1.
DR AlphaFoldDB; C5BW62; -.
DR SMR; C5BW62; -.
DR STRING; 471853.Bcav_2413; -.
DR EnsemblBacteria; ACQ80663; ACQ80663; Bcav_2413.
DR KEGG; bcv:Bcav_2413; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_0_1_11; -.
DR OMA; LMSPLHH; -.
DR OrthoDB; 1151822at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007962; 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 membrane; Cell shape;
KW Cell wall biogenesis/degradation; Magnesium; Membrane; Metal-binding;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..360
FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT /id="PRO_1000202060"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 284..304
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; 38857 MW; 72E3ADDA866D7C97 CRC64;
MIAILVSGAV GLLVSLFGTP LFIRFLVKRQ YGQFIRQDGP TAHFTKRGTP TMGGVVIIAA
TVLGYTVANI SAQRMPQVSG LLLLFLMIGL GVIGFLDDFI KISRQRSLGL NARWKIIGQG
VIGVTFSVLA LQFPNEQFRT PASTQVSFIR DTGIDLAFAG AAVGLVLFVI WANFLITAWS
NAVNLTDGLD GLATGVSVFV FSAYVVVTMW QSNQSCQVLS QVGPSCYETR DPRDLAIVTA
AIVGACAGFL WWNASPAKIF MGDTGALALG GALAGLSILT RTEFLAVIIG GLFVVIVLSD
VIQIGFFKMT RRRVFKMAPL HHHFELSGWN EVTIVIRFWL IAALFVALGV GIFYAEWVVG
