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Database: UniProt
Entry: A0A2T7TJJ7_9MICC
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ID   A0A2T7TJJ7_9MICC        Unreviewed;       764 AA.
AC   A0A2T7TJJ7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=DDA93_10580 {ECO:0000313|EMBL:PVE17429.1};
OS   Arthrobacter sp. Bz4.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=2171979 {ECO:0000313|EMBL:PVE17429.1, ECO:0000313|Proteomes:UP000244710};
RN   [1] {ECO:0000313|EMBL:PVE17429.1, ECO:0000313|Proteomes:UP000244710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bz4 {ECO:0000313|EMBL:PVE17429.1,
RC   ECO:0000313|Proteomes:UP000244710};
RA   Goncharov A., Nikolskiy P., Shidlovsky F., Kolodzhieva V., Zueva L.,
RA   Masharskiy A., Suvorov A.;
RT   "Putative ancient Arthrobacter sp. strain from the intact mummy of late
RT   pleistocene steppe bison (Bison priscus bojanus).";
RL   Submitted (APR-2018) 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:PVE17429.1}.
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DR   EMBL; QDAE01000012; PVE17429.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7TJJ7; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000244710; 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: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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244710};
KW   Transferase {ECO:0000313|EMBL:PVE17429.1}.
FT   DOMAIN          77..263
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          367..646
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          717..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  80946 MW;  6D63FC65AE20CDEE CRC64;
     MAARKSPIFD TATTLGKMIA FLGISALSGV LAAGLLVPVA AATGTGASAS IQFFEELPAE
     LERGALAQPS RILASDGTLI ATLYEENRQP VTLDQVSPNM VNALLAIEDA RFYEHGGVDL
     QGIMSAVVSN VSSDTTRGAS TITQQYVNNV LIDASLQSGD GSVTFSGGKT LGDKLREAKL
     AIAVEKELSK DEILEGYMNI VPFTGTTYGV QAASRYFFNV EAADLNIQQA ALLAGVVNGP
     TFYSPELNPE RSLERRNLVL GAMLSNSHIT QEEYDAAVAT DLGLDITPTL SGCVGAEQAP
     YFCDYVTHLI LNDPAYGESL EARQDTLYRA GLTITTTLDP VAQTAAQTAI NETAGRETTD
     PSVGHSMVSM EPGTGDILVM AQNTRYMPGT EPGDSVLNFN VDQYSGGDPN QPLGGVGGFQ
     PGSTFKPFIV AAWLEDGRAL NTTIDGRKRI YPQFDEWEAS CYPDGKYVLP DEDGYEPQNY
     GDINYGSYTV LEGLAQSYNT ITMETARQID LCMPFQIAAD LGIHDGKSAD GDYTPLTVSP
     SALIGGGSEV SPISMATAYA ALGAEGMTCE PRALTEVVAV DGTSFPVPEA ACEQAIPEEL
     ARGVNYATEA VMERGSGQLL EFGDIPMAGK TGTNDARSQT WFMGYNSGMA TATWLGNWKA
     NSVSLGELQI GGQIYPEIDG SFIAAPSWER FMQQIPGLHS GEPFTDPPQR MLNAQRPTIQ
     TQPGNGNQTG RPGDNQGSPG NSGPPADPPP GNSPEDPDNN EDEG
//
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