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Database: UniProt
Entry: A0A0R1KC97_9LACO
LinkDB: A0A0R1KC97_9LACO
Original site: A0A0R1KC97_9LACO 
ID   A0A0R1KC97_9LACO        Unreviewed;       876 AA.
AC   A0A0R1KC97;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=FD03_GL001205 {ECO:0000313|EMBL:KRK81068.1};
OS   Companilactobacillus nodensis DSM 19682 = JCM 14932 = NBRC 107160.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Companilactobacillus.
OX   NCBI_TaxID=1423775 {ECO:0000313|EMBL:KRK81068.1, ECO:0000313|Proteomes:UP000051248};
RN   [1] {ECO:0000313|EMBL:KRK81068.1, ECO:0000313|Proteomes:UP000051248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19682 {ECO:0000313|EMBL:KRK81068.1,
RC   ECO:0000313|Proteomes:UP000051248};
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:KRK81068.1}.
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DR   EMBL; AZDZ01000002; KRK81068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1KC97; -.
DR   STRING; 1423775.FD03_GL001205; -.
DR   PATRIC; fig|1423775.4.peg.1235; -.
DR   eggNOG; COG0744; Bacteria.
DR   Proteomes; UP000051248; 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; 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:SF33; PENICILLIN-INSENSITIVE TRANSGLYCOSYLASE; 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   Transferase {ECO:0000313|EMBL:KRK81068.1}.
FT   DOMAIN          49..221
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          354..590
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          782..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..802
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..833
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   876 AA;  99126 MW;  89E9D5541DE2B066 CRC64;
     MILVGTGLFW AKYGYDIKNN IADGYSYSQG LTKGDFKPKN STVIYDRNGK VIKKLSQSSS
     DYTPINEINP KITKGLVKVE DQRFYIHHGV DPYAILRSLV AKVMRRRIEG GSTLTQQLVK
     NVVLKDQSQT FNRKLKEMVI AQQLEKKFTK KQILEFYIND VYMGHGSYGF SSAANYYFSQ
     NQNDLSIDKI AMLVGIPNNP IYYDPVNYPH RSLLRRNMVL SIFYKNGVIN KSTYRNARKR
     PLGIKVNEHK YDNDVSNNYA LSYAVYNATE ELMKSSGFTL KYKFDTDAQR KQYNTEYQQA
     YERAHGELMD GGYSIHTSID MDIQNQIESI VAKQYAAYTG RDVHGKLAPQ VSSTVIDNKT
     GDVLAIVGGR TTEGDQVNRA IMGYRQPGSS AKPLTAYAPA FERGYLPQSS VIDSAVSSDS
     GHAITNWYSG YTGRTTVRHA LENSINTVAF KLASEDKDHT YYDDLTKMEF ARLTPQDNNP
     IIAIGGFTYG VTTTEMASGY SSFSRNGQFI HPSNLTSIYD TSHERYIYQN THLKKKIYSA
     DASYMTINTM QSVISDGLGK AAALDNYSHT AGKTGTTDNT KDSYFVGMTK SFTIANWTGN
     DVSSSLTGAE QSLPMSTFKA EGEYLVDQLK EKDTDFKKPS TVKVSGQDLT VVKSNKQPSI
     QDVIDTNFEK FNKKQESKND NRLYNMDYRI IYHLTKKEEF SREHKVQKAI DKYNETPIKK
     QSQYDKKLDE IQKIRYLNAN VKRQSAKIKF NNQILELQKD LNMSQAMFQS EKDNKKIAGY
     DAQKEDLEAQ RDKERKDKVA KLQTQYDSQL QKVKDAYKNN DSDKDDQKQK LIDIMNEIRS
     YGGNAPDLKL NVDSGSSSSN SSNSNSSSTT SDSTNN
//
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