ID A0A0F5VYK4_9ACTN Unreviewed; 792 AA.
AC A0A0F5VYK4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=TN53_15290 {ECO:0000313|EMBL:KKD07198.1};
OS Streptomyces sp. WM6386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD07198.1, ECO:0000313|Proteomes:UP000033641};
RN [1] {ECO:0000313|EMBL:KKD07198.1, ECO:0000313|Proteomes:UP000033641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6386 {ECO:0000313|EMBL:KKD07198.1,
RC ECO:0000313|Proteomes:UP000033641};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
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:KKD07198.1}.
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DR EMBL; JXTE01000020; KKD07198.1; -; Genomic_DNA.
DR RefSeq; WP_046259020.1; NZ_JXTE01000020.1.
DR AlphaFoldDB; A0A0F5VYK4; -.
DR PATRIC; fig|1415558.3.peg.2650; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000033641; 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:UP000033641};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..265
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 367..624
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 83701 MW; 3AF911AEAB5A0DA0 CRC64;
MSDEPQQPNQ GWAPREPQAA EEPGGKKPKR PKRTGWRRII PTWRMVLGTF VVGILLLIGL
FFLGYSLVKI PPANALATKQ SNVYLYADGS QLARDGEVNR ENVSLSQVSK AAQHAVLAAE
DRDFYSESAI DPKAMVRAGW NTATGKGTQS GSTITQQYVK NYYLAQEQTV TRKVKEFFIS
IKLDREKSKA EILEGYLNTS YFGRNSYGIQ AAAQAYYGKD ATDLSAAEGA YLAALLNAPS
EYDVVAHPQN KSAAVARWNY VLDGMVKEGW LEQSERTGLK FPMPKEATVS TGMSGQRGYL
VNAVNDYLSE NKILTADELD AGGYRITTTF QKSKQDAFVD AVNDKLMDKL DKKNRKVDTY
VRAGGAAVDP KTGQVVAMYG GIDYVKQYTN NATRRDFQVG STFKPFVFTS AVQNESTTQD
GRTITPNTLY DGTNKRPVQG WTGGSYDPAN EDDVSYGDIT VRTATDKSVN SVYAQMAVDV
GSDKVKDTAV ALGIPSNTPD LNASPSIALG VNTASVLDMA ESYATLANHG KHGTYTLIKT
ITRDGKDVVE LPEHKSSQVV TRQAADTTTS ILQSVVENGT ATAAQAAGRP AAGKTGTAEE
DQAAWFAGYT PDLATVVAVM GQDPVTAKHK SLYNVMGLPR INGGGAPTEI WAQFTEAALK
GKPAGEFDLE LQEGADVVET PTQEPSFVPP EDTEGEDNGG TTDGGQDTGG ETDGGTTGDT
TTTGGTTGDT TTGGTTGDTT TTGGTTGDTT TTGGTTGDTT TTGGTTGDTT TGGTTTGTTG
GTTAGGGPPT TQ
//
