ID A0A0F9YZ42_9BACT Unreviewed; 691 AA.
AC A0A0F9YZ42;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpB {ECO:0000313|EMBL:KKP36703.1};
GN ORFNames=UR28_C0039G0014 {ECO:0000313|EMBL:KKP36703.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_33_10.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619065 {ECO:0000313|EMBL:KKP36703.1, ECO:0000313|Proteomes:UP000034183};
RN [1] {ECO:0000313|EMBL:KKP36703.1, ECO:0000313|Proteomes:UP000034183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKP36703.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBOP01000039; KKP36703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9YZ42; -.
DR Proteomes; UP000034183; Unassembled WGS sequence.
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:SF15; PENICILLIN-BINDING PROTEIN 1C; 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 Glycosyltransferase {ECO:0000313|EMBL:KKP36703.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transferase {ECO:0000313|EMBL:KKP36703.1}.
FT DOMAIN 52..214
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 298..542
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 671..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 79514 MW; DDE26FC5440EE9B8 CRC64;
MKKILTIIAL ILSFIIAGFF TWANFASKNL LELYKQNEST IVTDRNNKII EILPNQKKFY
AIYTQKIPGN LKNLLIQKED QYFYYHLGLN PISKLRAIWR LFFNSKNTAS STITEQLTKI
LLNHENDRTG KNKIIEIFYT KALEINLSKN KILEMYLNSI FFGHNVQGIS LASRLYFDKN
SENLSNEEIC KLLATISSPT NLNPFIKNNK KEAEKIAGIL GLENLEINDF EKKEIQILEN
KFNNFITKKS AFEIKDLKLN KNLTKKNLTI DQDLNDKIRS IAKEKLSTLY EYNARNAAIV
VIKIPENELI AIVGTKDPYS DLNADQVNMA MKSRAIGSTV KPFIYTKGFE KDLRPYTLVD
DREYKYYTAG NFAHYPKNYD YQYHGIITLH IALSNSLNVP TLKVLEYVGL KNFYNFLSKD
LQFKSVQPLE TYEYGIALGN LEMDLLSLSY YFTIFPNNGY LKPLKTSNNG DLYFTPNKKI
FDEKYIELTN KILSDRNTGI DQFGMASNLN LPQKNFAVKT GTSQKFRDTW TIGYTPDFLV
GVWVGNADNS PMKELSSQIG AGLIWHDVMT LLLNSNYNKK TPFVFDQIQN FPNENTIEYG
LKNDDFEYHK NLLINPTLIL SPHNNDEFLF SENLQIPLKS NEELEWYING KFLAKGTEVI
WQPKIPGTYQ ISATNENKGK KGNYGGDRGL N
//
