ID A0A0A0JKM9_9MICO Unreviewed; 765 AA.
AC A0A0A0JKM9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=N803_11365 {ECO:0000313|EMBL:KGN37648.1};
OS Knoellia subterranea KCTC 19937.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN37648.1, ECO:0000313|Proteomes:UP000030011};
RN [1] {ECO:0000313|EMBL:KGN37648.1, ECO:0000313|Proteomes:UP000030011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN37648.1,
RC ECO:0000313|Proteomes:UP000030011};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia subterranea.";
RL Submitted (AUG-2013) 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:KGN37648.1}.
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DR EMBL; AVPK01000004; KGN37648.1; -; Genomic_DNA.
DR RefSeq; WP_052112035.1; NZ_AVPK01000004.1.
DR AlphaFoldDB; A0A0A0JKM9; -.
DR STRING; 1385521.N803_11365; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000030011; 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; 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:SF34; PENICILLIN-BINDING PROTEIN 1A; 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:UP000030011};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..271
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 364..609
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..765
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 82651 MW; 752503ED50B6B957 CRC64;
MSTAPPSRAE ARLLQEGRSS RGSGRGSGRG SGQGSGRGPQ RRGLSWPRRI LYTLIGLFVL
GVAGLGVAYA MTDVPDANAD AVSQANIIYY VDGKTEIGRI SELNRENVKL EQIPAHVQHA
MLAAEDHNFY QNNGISPSGI ARAVWVAVKG GEATQGGSTI TQQYVKNYFL SQDRTLSRKA
REILISIKID KQQSKDEILQ NYFNTIYYGR GAYGIQTAAK AYFDKDVSQL TPAEGAFLAS
AIRGPSYYDP RLGDQQKSNA ETRSGYILDA MVREGWLTPE QRAAATFPTT FKKYQPPTVT
GTNGYLVEEV KKELARTLKL SEQDISKGGL KIVTTIDKKK QDAAVDAIDE RIPESEKDLK
VGLVSIKPGD GAIQTLYGGA DYAKRQQSTA TQDTMQAGST FKIFALIAAL QSEKVSIRNT
FDGSSPQYFE EFEDEAAKTE FNRRGGVRNF NNQDYGRITV PTATANSVNT VYAQLNIIAG
PEKTAAAAKS AGITTKIQTN PGNVLGSDNV RVIDMANAYA TLAAKGIKST PYIVKSAQSN
DGTFDYKAKP QTTRVFDADL VSDVVYSMEQ VIERGSGEYA GSRLNRAAAG KTGTSSDNYS
AWFDGFTPQL ATAVGMYKGD GSVVKPDGTP NEENQMDDVE GWGAITGGTI PVRIWTDYMR
IATQGMEKLK FPEPAYINKD AAPKQTSRPR DANTSRPRDA NTSRPTSRPS QTEAPSSTAP
PTTSDPTPTE PTEPPPSEKP KPTKTPKPTI SIPLPPSPGT DQTPG
//
