ID E1KVL0_FINMA Unreviewed; 976 AA.
AC E1KVL0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9289_1404 {ECO:0000313|EMBL:EFL54890.1};
OS Finegoldia magna BVS033A4.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=866773 {ECO:0000313|EMBL:EFL54890.1, ECO:0000313|Proteomes:UP000003807};
RN [1] {ECO:0000313|EMBL:EFL54890.1, ECO:0000313|Proteomes:UP000003807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVS033A4 {ECO:0000313|EMBL:EFL54890.1,
RC ECO:0000313|Proteomes:UP000003807};
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:EFL54890.1}.
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DR EMBL; AEDP01000013; EFL54890.1; -; Genomic_DNA.
DR RefSeq; WP_002839070.1; NZ_AEDP01000013.1.
DR AlphaFoldDB; E1KVL0; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000003807; Unassembled WGS sequence.
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: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 64..236
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 513..769
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 530..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 110896 MW; 97CB1797913BAE53 CRC64;
MNKDKNIILK SIKILILCLI CIFAFVGGLI GVAGVRAMQL APKVNPEEIN NMMNQTSEIL
DQDGNLIEKI KTTEYREVVK LDKIPKYMMD AFTSVEDERF YKHNGVDPIG ITSAIFDNLR
SGSMKRGAST LAQQLARNLY LTNEKSFDRK FKEAYLAMEL TNYLGREKLL ETYMNTVFLG
QNAYGVQAAS EIYFKKNINE LTLSECATLA GIVKSPTNLA LYKAIEPGQV KDQSKIVGEV
TLSGETYKAV YNQQTIDRRD YVLKKMLENK KITKEEYETA LQENIVANIK PGIKNVDNLS
NYYSDIIYEQ VIAKLIEKGY SQQEAKSKLI NGGLKIYSCV DMNMQSNLEK LYDKKVDDII
SDGSSANLLK WSSDDGRNIT NALDEVIYFR KENIINDNDE FFISPKQYTK NPDGSITFNY
SKSIKVKQYG NYLDLKDYYS VNDSNNLVTH KISSINIGKK NLNTDGEGNI TISSQYIKDN
PNLIKYDNND NLIFNKDFYT INEDGIKQPQ SSSVVIDKST GQIKALVGGR YSDNKDTTNR
ASDIPRQVGS SMKPLGVYTP ALDNGYSPAS GLDDLPHYNE KHELWPKNWY EGYEGLVSLR
HAVENSINVT AVKVLEDIGI EKSKTYLEKF GLINAKNPKA DNYISAAENT SENDENTSAM
ALGSLTKGFT PVEMAGAYNA INNSGQYREP ISFTKVTDSL GKVIIDNPQK QNEVVSPQIA
YIMRDILRTS TDYNYSKYAR LDGFDIGGKT GTTTDYQDVW FVGMSPYYTI STWLGFDNQQ
LKMTQISQKK VVQIWSAVNK YTLEDKIPIK FDEPDGIVRV KVDTLANKLP SKYSWRDPRG
IVKEEIYKAG TEPTEVSDLY ESRRIDVVDG KLATDNTPPW ELGWGVFIKR DPPYKPSEHN
NIIPKDWKYS MPGYSDRTIF NIFKPKDKED EDKDDKDKDG KDKDEKDNKD NDKDNKRNNR
ERERKRDRDS SNDKRN
//
