ID A0A1I5W4K9_9LACT Unreviewed; 938 AA.
AC A0A1I5W4K9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN04488506_0768 {ECO:0000313|EMBL:SFQ14678.1};
OS Desemzia incerta.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae; Desemzia.
OX NCBI_TaxID=82801 {ECO:0000313|EMBL:SFQ14678.1, ECO:0000313|Proteomes:UP000199136};
RN [1] {ECO:0000313|EMBL:SFQ14678.1, ECO:0000313|Proteomes:UP000199136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20581 {ECO:0000313|EMBL:SFQ14678.1,
RC ECO:0000313|Proteomes:UP000199136};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FOXW01000002; SFQ14678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5W4K9; -.
DR STRING; 82801.SAMN04488506_0768; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000199136; 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; 3.40.50.12800; -; 1.
DR Gene3D; 3.90.1310.40; -; 1.
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:SF32; PENICILLIN-BINDING PROTEIN 2A; 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:UP000199136};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 97..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..339
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 495..762
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 41..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 103325 MW; AB03E6BCB5C04DD0 CRC64;
MNDSDNKDGR SLWEKISQYG KSVYQNSMSF IDSSREKIAG KNRAEEDALA AETSGNHEVD
EATELSSDNI DENKEPRTGF SKFLFGFNVA YNVIKNLVII FSLILLIGGA FAGGAGVGLF
ASLVSGQTPP SYEDMQVAIG NVEQTSTMYY ANGETISDFR SDLKRTTISL DDISEYVING
VIATEDEYFW EHPGVVPKAV LRAVVQQLTG SVQTSGGSTL TQQLIKQQIL SPEVTFERKV
NEILIAFRVE NYFSKEEILQ AYLNVSPFGR NSLGQNIAGV QEAATGIFGV NAKDLTLPQA
AFIAGLPQNP ITYSPYTGSG QVKEDQTSGL SRKNEVLFRM FREGYITEEE YASARDYDLT
QDFILRQENE QDTNSFAYDA VETEARLILM KLLYEADGLT KEDIDADPNL YTRYYERADD
DLRLNGYKVY STIDKTIHNA LEQVASEYGP GMGRTKKAPA VYDPSTGEYI QPMEEDPETG
ESVPKMVEIQ VGSSLVDNAS GRIIAFVGGT NYQDNMLNHG LYVERQPGST IKPVLVYAPA
LEEGLITPAS MVSDSRLFVP NWVNGRIEGH EVTNVGNVYS DKNVSARESL VNSMNIPTSR
IYLQMMENGS TPGNFLPLMG IGADAVHPDE YKNAALALGG TGHQEVNEEG EVVGMIYGPT
VLEMTSAYTM LANQGVHADP FMIERIENSD GEVIYQHESE TTKVFTPETA YMTVDILRDV
MENSTVGGTT DQLNFSADIA GKTGTTNAQE DIWFIGMTPT ITLSSWIGYD VDQISIDTEN
GVHPSKRNLN FWARLMNAVY EKNPTLVGSD KNFTRPEGIV EEEVLAETGM KPGEITVPSD
AVEKAKESEL QYADFEERKP NVSPSRWLPD GAKVSISGDM KKEIFAKDKV PGTTVYDFLI
GSPPHIQNSF WKSKAGSGAS AKAKENNENK EEENADED
//
