ID A0A267THG8_9BACT Unreviewed; 773 AA.
AC A0A267THG8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BWI92_06435 {ECO:0000313|EMBL:PAC31991.1};
OS Flectobacillus sp. BAB-3569.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Flectobacillus.
OX NCBI_TaxID=1509483 {ECO:0000313|EMBL:PAC31991.1, ECO:0000313|Proteomes:UP000215844};
RN [1] {ECO:0000313|EMBL:PAC31991.1, ECO:0000313|Proteomes:UP000215844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-3569 {ECO:0000313|EMBL:PAC31991.1,
RC ECO:0000313|Proteomes:UP000215844};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Flectobacillus sp. BAB-3569 genome sequencing.";
RL Submitted (JUN-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:PAC31991.1}.
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DR EMBL; NJFZ01000006; PAC31991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267THG8; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000215844; 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 Reference proteome {ECO:0000313|Proteomes:UP000215844};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..257
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 439..684
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 753..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 87712 MW; 3B1D0AFB602295A9 CRC64;
MIKLQPGKYQ RTIQSLWKWS IRGFIALVLY VLAVNYNFFW LFGGMPSLQE LENPKSQLAS
VLISEDGVEL TKYFRENRSP VEFEELSPNI INALMATEDA RFAKHSGIDL RSTFRVVTSF
GTAGGGSTIT QQLAKNLFNT RSAESAEEGM EYKGLLMRIP KISTVIAKTK EWILAIRLES
RYTKQEIMKM YLNEVEFGNN AYGIRVACKT YFSKEVGNVS VNEAATLIGM LQNPNLYDPR
RRPEKCLIRR NTVLAQMVKY GYLPESEAQD LQNQAILLKF KVENHNTGLA PYFREAIKKQ
LLAIIEDLNQ SRGDDEQLNL YTSGLKIHAT LDSRMQQYAE ESMREHMMAQ QKKFYEHWKG
RNPWVDEHMR EIKGFLKDAM KRTDRYRQLM EEMDGDEDKV WEVLKKPVRM TVFSWQGEKD
TTLSPLDSLN YYKRILNAGF MAMDPNNGHV KAWVGGINFK YFKYDHVRQS KRQPGSTFKP
FVYASAIESD IVTPCDYVVD EPVTFGQEDG IMKSWTPQNS DGKYSYQSMS LRRAMARSIN
TVSAKLMKQL GPQKVAEFAH RVGITSPLNE TPALCLGASE VSIFEQVDAY CSFVNEGYRI
EPLLILSIED KNGNELRRFE TTTKQVMNKE TAYKMVHMLQ GAVQEPGGTA EGLRRYSCAQ
GNEIGAKTGT TSNYSDGWFM GVTQSLVGGV WVGGDDRSIH FRSISLGQGA KMAMPAYAMF
MDKVYADPSL RIAGYKKGPF NKPDGVDINC YAAPSDSTQV QPPTVKPKDE DGF
//
