ID A0A346XYG3_9ACTN Unreviewed; 870 AA.
AC A0A346XYG3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DVS28_a2580 {ECO:0000313|EMBL:AXV07260.1};
OS Euzebya pacifica.
OC Bacteria; Actinomycetota; Nitriliruptoria; Euzebyales.
OX NCBI_TaxID=1608957 {ECO:0000313|EMBL:AXV07260.1, ECO:0000313|Proteomes:UP000264006};
RN [1] {ECO:0000313|EMBL:AXV07260.1, ECO:0000313|Proteomes:UP000264006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY32-46 {ECO:0000313|EMBL:AXV07260.1,
RC ECO:0000313|Proteomes:UP000264006};
RA Xu L., Wu Y.-H., Xu X.-W.;
RT "Complete genome sequence of Euzebya sp. DY32-46 isolated from seawater of
RT Pacific Ocean.";
RL Submitted (SEP-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};
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DR EMBL; CP031165; AXV07260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A346XYG3; -.
DR KEGG; euz:DVS28_a2580; -.
DR Proteomes; UP000264006; Chromosome.
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 CDD; cd06577; PASTA_pknB; 1.
DR Gene3D; 3.30.10.20; -; 1.
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; IPR005543; PASTA_dom.
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; PF03793; PASTA; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 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:UP000264006};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 700..765
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..870
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 92990 MW; E7C3861979B78543 CRC64;
MPSRTVGQTM RTDGDGCGDH HRTVRDCARV HRRPQAIGMS ETSPSSDRAL QLTKGGVLIL
LRTGGLFAGL LVGFLILGWV ASMLLAPAGE GLANSVGFGV QVPQEVELAG LDQTSTVYAA
DGSVIAVLHD EVDRTIVTLD EIPPHVQNAV LAAEDRRFYE HDGFDVEGFG RALLENLRTR
DVSQGGSTIT QQLAKSEVGD DISLQRKLTE VAFAMALERE LTKEEILERY LNQVYFGGGA
YGIAAAAEEY FAKTVGELTA GEAATLAGQI RSPGATDPRR FPDIALRRRD ATLRAMVQEG
WLPPEQLESE LNVPLQIAPR IIEQPSDPFI AEAVKQEFYT LEEFGDSRLE RNEVLLNGGL
NVYTSFDPRL QRIAEEVVLS YFPDPTPTAA LSSVDPRTGQ IRAIFGGSDF DREQYNFATQ
GRRQPGSGWK PLVMATALEI GFSPSMTLPG ASPTRFETGD EWEDRGVKNF GNASYGPITM
RRALVSSVNT AFAQLMLIVG PENVVNLANQ LGIDTNAALR DPVTGQVIIN PSIALGGLTN
GVTTLEMAGA FAAFANAGAW IEPSLIDRVE DQQGNVLYAR PTVPTQIFDP VVNEIMVDTM
QQVVCCGTAG RANIANLGWR AGGKTGTSQS NADAWFTGYT PVLSTSVWVG HPEGRIAMSG
VSSGRQPSQI WHDFMVQALE GVEPIEFPTE PPGGYEREVQ EGDVEVPDVR TLQEFDAYRE
LADVGLSART TEVDSERPAG QVVWQQPRGG SVVPAGEQIT IGISTGSVPP PPPPATPTDQ
PTAVPEPEPE PPTGPTDNPN PQEPLPGPPD NPQGRPTTDP APPPPPPPAP PPAPAPPPPE
PAPEPEPAPP PEEEEPPPPP DPAVGRPGGG
//