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Database: UniProt
Entry: A0A0R2JYG7_9LACO
LinkDB: A0A0R2JYG7_9LACO
Original site: A0A0R2JYG7_9LACO 
ID   A0A0R2JYG7_9LACO        Unreviewed;       654 AA.
AC   A0A0R2JYG7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-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=IV52_GL000522 {ECO:0000313|EMBL:KRN79117.1};
OS   Fructilactobacillus lindneri DSM 20690 = JCM 11027.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Fructilactobacillus.
OX   NCBI_TaxID=1122148 {ECO:0000313|EMBL:KRN79117.1, ECO:0000313|Proteomes:UP000051565};
RN   [1] {ECO:0000313|EMBL:KRN79117.1, ECO:0000313|Proteomes:UP000051565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20690 {ECO:0000313|EMBL:KRN79117.1,
RC   ECO:0000313|Proteomes:UP000051565};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN79117.1}.
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DR   EMBL; JQBT01000032; KRN79117.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2JYG7; -.
DR   STRING; 53444.AYR59_06060; -.
DR   PATRIC; fig|1122148.6.peg.542; -.
DR   Proteomes; UP000051565; Unassembled WGS sequence.
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   Gene3D; 6.20.370.110; -; 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; 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:SF32; PENICILLIN-BINDING PROTEIN 2A; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051565}.
FT   DOMAIN          35..206
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          304..549
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          605..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..625
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  71846 MW;  D517099855847CE2 CRC64;
     MTIIAKTSHV HNLQSNLSRS TLIYDKNGTK AGGLYSQKGT YVSSQKISPN IPNAILSTED
     RNFYHEHGFS VKGYGRAILL AIGNKIMGRN QISGGGSTIS QQLAKNTFLS QQQTLSRKFK
     ELFISIEIEN LYSKKQIITM YMNNAYFGNG VYGVQDASRK YFGMDAKNLP VQDAAVLAGM
     LQNPSNNPID HPEAAKQRRN VVLELMAENG KISKSELKNY QKLPLGTKDT FKVKDGYKYP
     YYFDAVINEA ISKYGLTEKQ IMNDGYKIYT NLDQQQQSSF QKDFKNPELF PQNAADGTKV
     QAASVAVNPK NGGVQAVVGG RNKDIFRGFN RATDIKRQPG STMKPLAVYT PALENGFNYD
     SKLVNKKLSY GKNNYTPNNY NNQYSGKVPM YEALAQSMNA PAVWTLNKIG VNKGYESVQK
     FGLPVTKKDD NLALALGGLS SGVSPQQMAG AYTAFANHGQ VSKPFYITKI VDSTGKTVGK
     HESSPSQIMS DDTAKQMTSM MMGVFDYGTG ATAKPSGYQI AGKTGSTEAD NSKDADATRD
     KWLVGYTPDV VVATWEGFDN TNSSHHLENL SGTGVNTLYK QQMEQIIPYT KQTPFKTQDA
     ATLVKEKDKQ NKHSSSKDKN DLAGKVQDFS KNVEVGAKSV AHNLIDGARS LLGR
//
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