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}.
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; 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
//