ID A0A2N0ERY8_9FLAO Unreviewed; 770 AA.
AC A0A2N0ERY8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ATE92_1011 {ECO:0000313|EMBL:PKA82871.1};
OS Ulvibacter sp. MAR_2010_11.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacter.
OX NCBI_TaxID=1250229 {ECO:0000313|EMBL:PKA82871.1, ECO:0000313|Proteomes:UP000232889};
RN [1] {ECO:0000313|EMBL:PKA82871.1, ECO:0000313|Proteomes:UP000232889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2010_11 {ECO:0000313|EMBL:PKA82871.1,
RC ECO:0000313|Proteomes:UP000232889};
RA Teeling H.;
RT "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT Genomic & Taxonomic Observatory).";
RL Submitted (NOV-2017) 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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:PKA82871.1}.
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DR EMBL; PHTY01000001; PKA82871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0ERY8; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000232889; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 22..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..246
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 430..687
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 770 AA; 86501 MW; 40E96C5C00217A27 CRC64;
MAKKQVRKTK APQNDERRNV RLFWKILGGI VGFIFLIFIL ASWGVFGSLP DETSLENPEK
NLATEIIASD GKVIGKFYQE NRTPVQYEEL PDHLIKALIA TEDVRFYDHS GIDAKGTVRA
FVFLGAKGGA STISQQLAKL FFTEQVSRNK LSRATQKIKE WIIATRLERR YTKEEIITMY
FNEYDFLNQA VGIESAANIY FDKAPSELTT VESAVLVGMF KNSSLYNPRR NPEGVRNRRN
VVLAQMAKYD FISETVKDSL QALPLNIKYT PQGHDEGLAT YFREYARAFM ADWIKANPKT
DGSKYDIYSD GLKVYTTIDS KMQEYAEQAV DMHISHLQKE FNKQNEKNKT APFRDITEQE
TDDILKNSMR RSDRWKELEK QGKSEAEIVK SFSKKTAMTI FAWGGDKDTI MTPLDSIRYY
KSFLQASLMS MTPQTGEVKA WVGGINYKHF KYDMVKKGKR QIGSTFKPFV YATVIDQMHM
SPCDTLPNTQ WTIPAGKYGL IKPWTPKNAG GGYGGMVTLK NALANSINTV TARLIDRVGP
RPVIDLVKKM GVDTKEMPEA PSIALGTPDV SLYEMVGAYS TFANEGVFVK PTLITRIEDK
NGTVLFQNVP ETKDVISNET AYVTVSLMEG VTQSGSGQRL RHTWAVGNAA YKNAVTGYPY
AFENPIAGKT GTTQNNSDGW FMGMVPNLVT GVWVGGEDRA VHFNSTTYGQ GATMALPIWA
IYMRKCYENE ELGISKGSFK RPANLSIVTN CAEYREGNSD VEGIPDEFDF
//
