ID A0A136MF42_9BACT Unreviewed; 737 AA.
AC A0A136MF42;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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=pbpD {ECO:0000313|EMBL:KXK32532.1};
GN ORFNames=UZ16_OP3001002526 {ECO:0000313|EMBL:KXK32532.1};
OS Candidatus Hinthialibacteria bacterium OLB16.
OC Bacteria; Candidatus Hinthialibacterota.
OX NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK32532.1, ECO:0000313|Proteomes:UP000070296};
RN [1] {ECO:0000313|EMBL:KXK32532.1, ECO:0000313|Proteomes:UP000070296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB16 {ECO:0000313|EMBL:KXK32532.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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 -!- 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:KXK32532.1}.
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DR EMBL; LMZT01000130; KXK32532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MF42; -.
DR STRING; 1617433.UZ16_OP3001002526; -.
DR PATRIC; fig|1617433.3.peg.2722; -.
DR Proteomes; UP000070296; 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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 7..146
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 228..495
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 650..734
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 584..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 81442 MW; 7DE50AA67EF00D87 CRC64;
MPRINVFYYH PGFDPIAILR AAWSNLREGR VVSGASTLTQ QLVRSAYPRP RTYLGKVCEI
IRAIKAEWLL SKEQILEQYL NRIPMGNNLV GVRLAAQCYF GKSLVQLEDQ EIAMLAALPK
APGRLNPYRQ PQDRLLARRN WVLQRMNEMG DLSSLNLAQA LEKPVAVRPI RFDTKAPHLV
HAISKKRPES AGEQKIRTTL AMALQEKVES VLRSHQMDLM SHGATQAAAM VVSNRNMAVL
AYVGSIEYSE KTLANNNGLT ALRSPGSALK PFLYAMALDA GYSAATLLED TRRHYRAPQG
EYYPRNFDQR EYGPITIRQA LGNSLNLSAI RMIDLTGVKP FYSLLKSIHL LDHTDKGPEF
FGLGLAIGNP EVTLENLVAA YAMLASGGKW RPLRFLREEP VDPGIEILQP ETSFIITDIL
SDPGARSLTF GGIADLNFPY RIAFKTGTST HYRDCWIIGY TPDYTVGVWA GNFDGSPMEE
LGGALGAGPL FSEIFQAIYP KKSQPEPFEP PSGVCQIAVC SHSGMLPTPY CPLQRKEWFP
VESTPLRSCT FHTRDTLYHE LNPTYAGWLY DRIARGQTTP YRLQGNPGLL LANEMEGPDP
SSPAHPEVTS PNLPAPSSPA PIPAPSTPSG ISSSPIRIGE ASGISNSGSP SPGTVRILYP
LEGDCFLLDH RRSEPQVIRL EARVDGSLET VTWFLDGMEY AQTGPPYRTP FELVRGEHIL
MAVVPGGSGD QIRFRVE
//
