ID A0A387BNZ3_9MICO Unreviewed; 797 AA.
AC A0A387BNZ3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=D7I44_12060 {ECO:0000313|EMBL:AYG04192.1};
OS Gryllotalpicola protaetiae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Gryllotalpicola.
OX NCBI_TaxID=2419771 {ECO:0000313|EMBL:AYG04192.1, ECO:0000313|Proteomes:UP000275069};
RN [1] {ECO:0000313|EMBL:AYG04192.1, ECO:0000313|Proteomes:UP000275069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2DFW10M-5 {ECO:0000313|EMBL:AYG04192.1,
RC ECO:0000313|Proteomes:UP000275069};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 2DFW10M-5.";
RL Submitted (SEP-2018) 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; CP032624; AYG04192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387BNZ3; -.
DR KEGG; gry:D7I44_12060; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000275069; Chromosome.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000275069};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..296
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 405..667
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 303..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 85171 MW; AED95F7AD61574C7 CRC64;
MSLSGSEAGR RTRLAKALGG FLGMSAIAGV LVGVLIAPAA IAGTTVTKSG IESFNALPDY
LKIEAPDQYT TFYATQNDQW VKIAQFYYQN RIDVPWDQVS QSVKDAAVAT EDPRFYSEGG
VDVLGILRGA ASTVSGNGTQ GGSSITQQYV KNVLVQRCEA DYPIDANAST KVRTEQQKKL
SACYQDAAGV TVPRKIQEIR YATGVSKQYS KQQILLGYLN LVGFGGQVYG VQAAAQYYFN
TTAAKLDLNQ SATLVAILNN PANLRIDQTK AQNPGSNPEN GFKATKDRRD YVLDRMVKNH
KITQKQADDT KKQPITPTIT PTPTGCTSAQ ANDAGFFCDY VQDTILNDTT FGKTAADRER
FFRRGGINVY TTLNLDLQNT AQASLDQYIP HSTGDPSFPL GASNVSMEVG TGRVVTMVQN
KTYSAGATSD PGATSLNYNT PYAYGGSSGF QTGSSFKPFV LAEWLEQGHT LYQSVNGSST
TFAYNKYQTQ CNSTAPYQSY GTFSVKNDTP SENGVRTVLQ GTAQSINTIY MMMAQQLNLC
DVHHLAQSMG VDVANPNKKT GGGTWSTSPT SAIGTNNVSP IQMAQAYAAF ANGGITCTPI
VIDKITRTDD GSNVAVPKTK CTQTIPKDIA DGVIYALKTV LTGNGTGVLA NPHDGVPLFG
KTGTSNDAIQ NWIVTSSSKV AQATWVGNLQ QNPSKSLRKT GFRGVTNHRY VQGGDAKLVV
AEPIIAALNK VYGGENWDAP PSSMLYGKNY KPPVTTAPTA PATTPAQPTQ PTQPTQQQPT
QPAEPQNPVV PLPTPSG
//
