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Database: UniProt
Entry: A0A1G7QKR2_9ACTN
LinkDB: A0A1G7QKR2_9ACTN
Original site: A0A1G7QKR2_9ACTN 
ID   A0A1G7QKR2_9ACTN        Unreviewed;       708 AA.
AC   A0A1G7QKR2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-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=SAMN05660662_4066 {ECO:0000313|EMBL:SDF99094.1};
OS   Blastococcus aurantiacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1550231 {ECO:0000313|EMBL:SDF99094.1, ECO:0000313|Proteomes:UP000199406};
RN   [1] {ECO:0000313|EMBL:SDF99094.1, ECO:0000313|Proteomes:UP000199406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44268 {ECO:0000313|EMBL:SDF99094.1,
RC   ECO:0000313|Proteomes:UP000199406};
RA   de Groot N.N.;
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; FNBT01000009; SDF99094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7QKR2; -.
DR   STRING; 1550231.SAMN05660662_4066; -.
DR   Proteomes; UP000199406; 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: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   ECO:0000313|EMBL:SDF99094.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          39..210
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          303..562
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          599..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..673
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..697
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   708 AA;  75027 MW;  B2B79009D7B25AA6 CRC64;
     MLLCVFIGVV YASTEVPSPD SITSAQTTVV YYSDGTTEMA RLGDENRTNV RLDQVSEAAQ
     NAVLAAENRD FYTDPGISAT GIARAAWSNL TGGSTQGGST ITQQYVKNAI LENSERSFSR
     KFQELFVAIK LDNNYSKEQI LENYLNTIYY GRGAYGIESA AKTYFGVPAA ELTAEQAAVL
     AVLIRSPGAY DPELNPEGAQ DRWGLVLDAM VGEGWLSAEE RALSQYPLVL PKVPPSNGIP
     NDSRGHVVNR ALAELAAKGY TEDQINGGGL RIVTTVDKRY QDAAETAVND VMTGEPEQLR
     EALVAVDPKT GAVRAYYGGE NGAGFDYAQS PRQPGSSMKP YALATALKDG ISVTARRNGS
     NNQTFEDREA PVVNSGGASC GSCTLREAMT RSLNTTYYGL ALEVGADKVR ETALAATGLP
     DVWDAGGELF LRKPTLANRD GFTGAAIGIG EYEMRPIDQA VGFATFASGG IRRAPYFLAR
     VTDSEGTVLL DNPGDPGQQV IEPRVANDVT YALTDVARSS DLALAGGREV AAKTGTQGLN
     RTDNSDAWMV GYTPSLSTSV WIGTDVRDPI RTVGGSIIYG SGLPGDIWQQ FMNTVLEGTP
     EENLPDAPLI KGDTGEGVPE PTQQPTRPTS SAPSSSAPST RTSTPARPTA PVEPEEPADT
     GEEEPEEETE ETTTPENPST TPTSPVRPVP PVNQDGAPAP DPAGRGNG
//
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