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Database: UniProt
Entry: A0A346XYG3_9ACTN
LinkDB: A0A346XYG3_9ACTN
Original site: A0A346XYG3_9ACTN 
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
//
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