ID A0A0D0X4D7_9ACTN Unreviewed; 965 AA.
AC A0A0D0X4D7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=TK50_01435 {ECO:0000313|EMBL:KIR64380.1};
OS Micromonospora haikouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR64380.1, ECO:0000313|Proteomes:UP000032254};
RN [1] {ECO:0000313|EMBL:KIR64380.1, ECO:0000313|Proteomes:UP000032254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR64380.1,
RC ECO:0000313|Proteomes:UP000032254};
RA Long Z., Huang Y., Jiang Y.;
RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT genome.";
RL Submitted (JAN-2015) 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:KIR64380.1}.
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DR EMBL; JXSX01000001; KIR64380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0X4D7; -.
DR PATRIC; fig|47853.6.peg.311; -.
DR OrthoDB; 3397599at2; -.
DR Proteomes; UP000032254; 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:UP000032254};
KW Transferase {ECO:0000313|EMBL:KIR64380.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 262..441
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 555..836
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 100191 MW; 0AD291B3119F3EB6 CRC64;
MNSYGDPSSS RGRAQIPGAH GDPGAGPADA YRRGDDARGS WSEGTAQPGR ASVPPRGQAA
GGRASVGGSA AVPPRVGSAA VPPRAGSAAV PPRGGTAAGS ASVGSASVGR AGAGRASVPV
SPAPAAGRAG AGRASVPVSP APGGRASVGA AAVGGLAGRA SVGRAGVASV PGGPGGPGGP
GGPGGPVGPA GGRSGRGARD PGASARAKKR RRINMMIAGF AVFIMLAGIG VVSFTYYSTT
VVLPAQVPLP LSTTVYAKDN KTVLAKLGSE NRQLVKITEI PEHVQHAVAA AEDRNFYRHS
GVDYKGIARA AWNNLSGGDK QGASTITQQY ARNAYENLKD DSYARKVKEA ILASKLNDKY
SKPEIMEHYL NVIYFGRGAY GIEAAAQTYF GVHTKQLTVA QAAVLAGLIK QPVASDTHQG
YDPAVNPVDA KSRWTYVLDG MAAEGWIDAP NTPKRPTDAE YPKTLSPKKA GSAAFGVASP
RGNVINYVRQ EMDQWGICSD SGAAGKISCV DALRDGGYRI QTTIDPKLQT AAENTAMRAK
KNSELNDQPK NLMAAVVSIE PNSGRVLAYY GGDSGADFDY AGKNTDKNGD LVGGHQPGSS
FKVYTLAAAV NAGISVKSHW DATPFKPEGF DSPVQNANRD VSRTCGKWCT LEFSTIQSYN
VPFFHVTEKI KPSAVLDMAK QAGVSTIWTV DPPKAYDLNK NDPKDLAPSK FDRVIGYGQY
PVTVLDHANG LATLANDGKY NKAHFVIKVE KQNVDTGKWE MVASEKLKPQ QRIRADVAKE
VTGVLKQIPG PNNRSLDGGR EAAAKTGTWE YDSRHNAHAW MVGYTPQLAT AVWVGSRDPK
KPQIIDKDGN DIGGSKLPGA IWQRYMNAAL NGKDKESLPA ATGMGDQDAG NGTEPPPPPP
TTPEVPNCNP LDIFCQNPTN PGPGGPNNPG GPESPTPPGG DPTDPRPGGG NGGGILPTLA
PRARE
//
