ID   A0A1G4XV52_9ACTN        Unreviewed;       770 AA.
AC   A0A1G4XV52;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN03159343_1497 {ECO:0000313|EMBL:SCX44920.1};
OS   Klenkia marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Klenkia.
OX   NCBI_TaxID=1960309 {ECO:0000313|EMBL:SCX44920.1, ECO:0000313|Proteomes:UP000198981};
RN   [1] {ECO:0000313|Proteomes:UP000198981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45722 {ECO:0000313|Proteomes:UP000198981};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FMUH01000002; SCX44920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4XV52; -.
DR   STRING; 1960309.SAMN03159343_1497; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000198981; 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   CDD; cd06577; PASTA_pknB; 1.
DR   Gene3D; 3.30.10.20; -; 1.
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   ECO:0000313|EMBL:SCX44920.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          69..254
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          348..649
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          736..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..770
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  79802 MW;  966343395940A2B7 CRC64;
     MSVARRIGTL AQLLGAVVLA GVLVAAVLFP VVGGLGVTAR NSASLLDALP VELTDRTPPG
     NTVLLAANGE VITGFYDENR APVAADRIAE VMKQAMVAIE DARFYTHNGL DVQGTLRAAV
     TNVVAGDVRE GGSTLTQQLV KQTLLQTAET PEEAAAATEQ TLDRKLREAR LALALEQTYS
     KDEILTRYLN IVYFGQNAYG VQAAARIYFS VDAADLTLPQ AAMLAGLAQS PTNDDPTVNP
     EAATTRRDQV LDRMAELGTV SAADAAAAQA EPIVLALGAP PPRGCVQASV GPFVCDYVQR
     YLTQTLGLTQ DQLEHDGLTI QTTLDPDLQR AGDAAVLETL PMGDSLAGLF TAVQPGTGHL
     LAMSVNRVFG YDVTDPAQES YNLNVAASQG SGSTYKVFTA AAALARQYSQ YYTLTTSDPY
     VSRVYRDGSE PYDVRNAGRY SPTLDLATAL YQSSNTYFLA LEDALGSVEE PVRMAEAAGL
     FQFSRPGLAQ QIIDENRGSF TFGAEETSPL ALASAYSTFA AGGTRCLVTP VTAVLDRFGQ
     PVTGADGQPI VRGDQCTPEA IPSGVATTMN QILRRDVEPG NPGQTGSRAY VPGHQIAGKT
     GTSQDNYSAA FVGYTPEITA SVMVLNPKQN QDVGGFGGNK PATIWRAAMA PILEARGSGE
     FPPADPSVVN GNTLPVPGCG SVSACRSALA GAGFVPQTVT VDGDRPAGAL LGTSPPAGGR
     AVVGQVVTIR VSNGSAYTAP APAPAPAPAP APAPPGPPGG PPSIPGQPVG
//