ID F3P828_9ACTO Unreviewed; 673 AA.
AC F3P828;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9056_01196 {ECO:0000313|EMBL:EGF55704.1};
OS Actinomyces sp. oral taxon 170 str. F0386.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=762963 {ECO:0000313|EMBL:EGF55704.1, ECO:0000313|Proteomes:UP000004404};
RN [1] {ECO:0000313|EMBL:EGF55704.1, ECO:0000313|Proteomes:UP000004404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0386 {ECO:0000313|EMBL:EGF55704.1,
RC ECO:0000313|Proteomes:UP000004404};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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:EGF55704.1}.
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DR EMBL; AFBL01000035; EGF55704.1; -; Genomic_DNA.
DR AlphaFoldDB; F3P828; -.
DR STRING; 762963.HMPREF9056_01196; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_6_11; -.
DR Proteomes; UP000004404; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 61..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 350..620
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 673 AA; 71471 MW; 766C41B42DE9934C CRC64;
MLVVFLTLSG VGGVLSAGFA TPFVGVTAAL TKASAELFEE LPSDFNVQQP SQISTLLAAD
GSEIAQFYAE NRIVVPLSEI SVNMQNAIVA VEDQRFYQHQ GVDPTGMVRA LVSNNSGGSR
QGASTLTQQY VRNTLIETGL KNDDHKIIKD ATESTVARKL REMKFALSLE QKYSKQQILE
GYLNIAAFSP STYGVEASSL HYFNKHAKDL TVAEAALLAG TTNAPSAYDP ESQPELAKNR
RDWVLSKMLE EKFITQEQYD EAVSSEIQLD VQEAPAGCGA AGNYAYFCTY VVNEILGSEN
FGPDVASRRQ LLTRGGLKIT TTLDRARQNA ADGIIQANTP IGDSDGANST IVSVEPGTGR
IQALAQNTNY EDSQLVFAAD AKHGGVELPD GNVGFQPGST FKALILAEWL KTGHTAGQTV
NASAPRTYPP NTFNIPCAPE LAAGSWTVNN VAGTNAGNMS VRDATKQSIN VGFTEMLRQL
DVCDVTQFAA SIGVSKADGS QLDPDPSLAL GAKPVPPLSM ANAYATFASG GKYCKPVAID
SILDASGTSM AVPSADCTQA MDQNVADQTA ITLQATSEPN GTAKDAGIGR AIAGKTGTTD
EAENAWFVGF TPQLSTAVWI GDAKESNKSL AGRTIGGKYF ERMYGSDLAV PMWRDYMSQA
LANEPAVQIP HHP
//
