ID A0A3E2YLZ3_9ACTN Unreviewed; 755 AA.
AC A0A3E2YLZ3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpG1 {ECO:0000313|EMBL:RGC67249.1};
GN ORFNames=C5N14_19835 {ECO:0000313|EMBL:RGC67249.1};
OS Micromonospora sp. MW-13.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2094022 {ECO:0000313|EMBL:RGC67249.1, ECO:0000313|Proteomes:UP000258607};
RN [1] {ECO:0000313|EMBL:RGC67249.1, ECO:0000313|Proteomes:UP000258607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW13 {ECO:0000313|EMBL:RGC67249.1,
RC ECO:0000313|Proteomes:UP000258607};
RA Jahanshah G., Miess H., Busche T., Ruckert C., Kalinowski J.,
RA Rokni-Zadeh H., Gross H.;
RT "Draft Genome Sequence of Micromonospora sp. MW-13, a Bacterical Strain
RT Isolated from the Rhizosphere of Wheat in Iran with antibacterial and
RT possibly plant growth promotion properties.";
RL Submitted (MAY-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:RGC67249.1}.
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DR EMBL; QKKX01000038; RGC67249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2YLZ3; -.
DR Proteomes; UP000258607; 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:SF33; PENICILLIN-INSENSITIVE TRANSGLYCOSYLASE; 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:UP000258607};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..280
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 386..690
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 705..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 79807 MW; F1E6DDCE445F5757 CRC64;
MNYLTIGPGA GRIAAFMAIL GFMPPPRSPL SRLFTVLLAG VLAGLVLAVA ALPGNLLLGF
AAKSAIGSYA ALPEALRTPT TPQRSYLYAN DGETLITTFY DVNRTDVPLA EIAPVMRQAI
VAAEDRRFYS HGGADLRGLA RALVANVTGG GTEQGGSTLT MQYVRNVLKT DPNRTAEERQ
AATEQTVGRK LQEIRYATAL EQRLSKDEIL NRYLNIAYFG SGAYGIAAAS QRYFAKSPAE
LTLPEAALLA GLVQSPDAYS PIDGDADAAL ARRGYVLDAM AGTGAVTAEQ AAAAKAEKLV
LSPTRQPNGC TAVAQGHDDW GFFCDYLRQW WLTQPAFGDT VPEREQALRR GGYTVVTSLD
PKLQATAQQQ ATAVYGYDNK RALPIAAVQP GTGRVLAMAV NRHYSLDPNP DGKVNRPNTV
NPLVSGGGGV DGYQAGSTFK LFTMLAALES GRQLATGFDA PSRLPTRYAA EGEASCGGKW
CPANANPQWM DGYRTMWDGF GRSVNTYFVW LAEQVGPAKV VEMAQRLGIT FRADADAAFA
KDNAANWGSF TLGVAATTPL DLANAYATVA AEGTYCAPLP VVSVTTADGD PVPVGEPSCR
QVLDADVARA ATDAARCPVG QQTTFGQCDG GTATSVDRIV GRPVAGKTGS SEKNATETFV
GFTPQVAVAG IAANPDDPSD PVGSAVQARV IDAVARTIRT AVAGQPVRDF TPPSRALAGE
VHRPAPQPSP PQQQRRQQDQ NLPPDVLRWL NRGRG
//