ID   A0A1I2ASU7_9BACI        Unreviewed;       951 AA.
AC   A0A1I2ASU7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN05216238_11740 {ECO:0000313|EMBL:SFE46658.1};
OS   Lentibacillus persicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX   NCBI_TaxID=640948 {ECO:0000313|EMBL:SFE46658.1, ECO:0000313|Proteomes:UP000199474};
RN   [1] {ECO:0000313|EMBL:SFE46658.1, ECO:0000313|Proteomes:UP000199474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22530 {ECO:0000313|EMBL:SFE46658.1,
RC   ECO:0000313|Proteomes:UP000199474};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOMR01000017; SFE46658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2ASU7; -.
DR   STRING; 640948.SAMN05216238_11740; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000199474; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 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   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          689..766
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|SMART:SM00060"
FT   DOMAIN          783..860
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|SMART:SM00060"
FT   REGION          563..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..951
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   951 AA;  102350 MW;  F67208D4982CFA23 CRC64;
     MATNGQSRTA RRKQKKATKK PLWKKLLMII GIAILVIGIG VGTLFTYYIV TAPDIDASKL
     ETPFSSKIYD KDGELFADLG AGEQRTKVEY DELPQVLIDA VLSTEDARFY DHPGVDIWRV
     GGAVVANITN GFGSEGASTI TQQVIENSFL SPEKKISIKV QEMWLALQLE RDYSKEEILE
     MYLNKIYYGN RAYGVGKAAE LYFGKTDLSE LTLPEAAILA GLPQRPSAYN PFKNPDLMKD
     RMNTVLNLMV ENDTISESEA EEARQVDIPS LLTDDTPDPT PYQAFLQQVT KEVKEKVQGA
     DVYTDGLKIH TTIDTDAQEH VEFLLSDSED NPVNYPEAVT DEEGNEHEME AGMTVLDTST
     GAIRAIGGAR GGLENDGLNY ATDISRQPGS TFKPIIGYGP AIEELQWSTY HQLNDDGPYD
     IAGSDKQINT WAGQYYGWVT MRYALQQSLN VPAAKTFEEV GGSTAKQFAE GLGISFGDND
     ILVGDVLGGN IGTNPLDLSG AYRAFANGGV YNEPYAVTKV EFPDNGRTVD TKPEPKAAMS
     EATAYMISDM LQTAIEDGTG AQANVPGLPD AGKTGTTTRE NVEGSPDSWF SGYTTNYTIS
     IWTGYNDNNI TLPDTKIPHA LYKNTMSELS SGIDTADFSK PDSVVEVDIE DGSRPAKLPS
     DYTPESEIVT ELFIEGTEPS ETSEEFDQLD PVEGLEADYD EESETIQVGW DYDSEEDVSF
     EVSASIDDGE MQGLSSTDDT TMEISNVESG ATYEIQVVAT TDSNTSDPAT TTVQIPGGEE
     EDIPAVSGLS ANPSGSAIDV TWQYNGPPAN FEVAVSQGGS EIQSQTVESQ GIVIEGAGVQ
     PGQTYRIAVT PVGQNGANQG VRGEQSSTEV TIPSDEQSNG SDNEDEGEDT DGGNNGENGN
     GEENSDNGDD NNDNGNNGNN NNGNESNNGN GDENGEENGN SPNAGNSGIE N
//