ID E7MP81_9FIRM Unreviewed; 890 AA.
AC E7MP81;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9430_01361 {ECO:0000313|EMBL:EFW23986.1};
OS Solobacterium moorei F0204.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Solobacterium.
OX NCBI_TaxID=706433 {ECO:0000313|EMBL:EFW23986.1, ECO:0000313|Proteomes:UP000004097};
RN [1] {ECO:0000313|EMBL:EFW23986.1, ECO:0000313|Proteomes:UP000004097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0204 {ECO:0000313|EMBL:EFW23986.1,
RC ECO:0000313|Proteomes:UP000004097};
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 (AUG-2010) 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:EFW23986.1}.
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DR EMBL; AECQ01000028; EFW23986.1; -; Genomic_DNA.
DR RefSeq; WP_006526169.1; NZ_GL637665.1.
DR AlphaFoldDB; E7MP81; -.
DR STRING; 706433.HMPREF9430_01361; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_5_9; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000004097; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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:SF29; PENICILLIN-BINDING PROTEIN 1A; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000004097};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..253
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 349..588
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 890 AA; 97922 MW; 56525D5398538A4C CRC64;
MTNKQTKKPG VKRKIHGFRI LTLFMAIIVG FEFVGAAVGA IAISTLLKGT PQFKLDDFTN
FQSTIVLDAN GTKIADVGQT LRENVVYNQI PEAMVDAFLS IEDSRYFSHN GFDIPRFTKS
IIETVLRGYM QGGSTFTMQL VKLTYFEDDQ AGTSKTKNIQ YKVQQIALAM ELEKNSSKEE
IFTMYLNKMN FGGVGNIRGV QKASLQYFGK NVWELNLAEC ALLAGVINSP YTFDPHNYLD
KATARRNTVL DMMLYHGYIT QEECDLAKSI KVEDLLIDAK STINTDYTYQ AYIDAALKEA
REVTGLDPMN VSMEIHTNMN PTVQAQLESI QAGTGGIDFP DDLYELGSIV INNQTGEVVG
IMGGRNWASG GSMLLDHATE QFNQPGSTIK PVLDYALAFE DLGWATSHTV LDKPVTYGNW
TFNNFDNTKW GVVDLSKAVG LSLNTVAINT LQAVIDKSGA QRVTNYLTSL GLSQFKPELF
DISFAIGGGN MRVSAQELAA ATGVLINGGN YIKPHTINTI FYRNGQKEPY VAPTTGTSVL
SPQAAYLASY LMRNAVEQDW GNYMYAIRKG YPVYGKTGTT DWGDAGLEYG IPVGAAKDEW
MVGQTTKFTI AVWSGYEKAI AGADTYFSRW KLNMNIPGVI ISNVLDTLES IYGTPGELAM
PEGISKITHI KGLYPYVAPD DTIPSDYVST GLVKTEYAKL GTYTNLITTP QNLASFTASY
DENNDTVNFA WTPYPDPAKL VEESHDDKTF DISWITGPIT YKARIVQNSA VVATINYTGD
KLSKVIDGLQ PDTDTQVCGY YGYEKNDTVA SNEVCVSFRT PEAKVTVPNY SDPRQYVEWG
NANGITINRA VGDTIASMSG RVQDVRDSNG NSVIGKKVKK GSTVTVYIYF
//
