ID E1L4W0_9FIRM Unreviewed; 695 AA.
AC E1L4W0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9321_1255 {ECO:0000313|EMBL:EFL56587.1};
OS Veillonella atypica ACS-049-V-Sch6.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=866776 {ECO:0000313|EMBL:EFL56587.1, ECO:0000313|Proteomes:UP000004211};
RN [1] {ECO:0000313|EMBL:EFL56587.1, ECO:0000313|Proteomes:UP000004211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-049-V-Sch6 {ECO:0000313|EMBL:EFL56587.1,
RC ECO:0000313|Proteomes:UP000004211};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
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:EFL56587.1}.
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DR EMBL; AEDR01000019; EFL56587.1; -; Genomic_DNA.
DR RefSeq; WP_005376275.1; NZ_AEDR01000019.1.
DR AlphaFoldDB; E1L4W0; -.
DR eggNOG; COG0744; Bacteria.
DR Proteomes; UP000004211; 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 343..576
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 75422 MW; D343CED718DC796C CRC64;
MGNNSNIRAR RKPAPNPSNP KASTKKTIWM IVLLLVLIVA GGGCGFISAT MSNLPDVSNV
RPSASSQIYD VHGNLITTVH STENRLPVPI NEVPKELQDA FVATEDSRFY SHHGIDPIGI
LRAIWVNVVH SGVSEGGSTI TQQLARNAFL SQDRTLKRKI SEALLALKIE QHYTKQEILE
MYMNQIYFGQ GAYGVQSAAH VYFGKDVRDL TLAQCAMLAG LPQSPNYYSP FNNLEAGKKR
QAVVLGQMVK YGYLTQDKAD AAREADLGLV AKQEQTHENN NASYFINYVI AQISEKYGDD
AIYKDGLKIY TTLDMDAQNA AVAAMQNLPT MYTDQNGLHQ PQGAIVAMNP HNGYIVAMVG
GRGDDAFNRA SQAERQPGSA MKPFVYLAAI QSGKTPGSIV DDSPVDFNGW RPQNYERNYE
GNITYRYALQ HSRNVPAVKI ADEVGMSKII DLAKKMGITT LTDEDNNLST ALGGLTHGVS
PLEMAEAYGV LANGGVKVQP TAIIKIVDRN GQVVEENSIQ EKRVVEEKDA AIITDMLESV
ITGGTGGNAA IGRPAAGKTG TTDDEKDAWF VGYTPDLVAA VWIGDDYGSE TLGITGGSTP
AVMWRQFMSA ALANTPASDF NVPASAQAAI SEGHYNPVKE APKKDDKDKK DDKDKKDGKD
KNDAISKDDD SSSKVESTDS KPSQSKSKKE KKKDR
//
