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Database: UniProt
Entry: A0A2R5HJL8_9LACT
LinkDB: A0A2R5HJL8_9LACT
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ID   A0A2R5HJL8_9LACT        Unreviewed;       760 AA.
AC   A0A2R5HJL8;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=NtB2_00603 {ECO:0000313|EMBL:GBG96491.1};
OS   Lactococcus termiticola.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=2169526 {ECO:0000313|EMBL:GBG96491.1, ECO:0000313|Proteomes:UP000245021};
RN   [1] {ECO:0000313|EMBL:GBG96491.1, ECO:0000313|Proteomes:UP000245021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NtB2 {ECO:0000313|EMBL:GBG96491.1,
RC   ECO:0000313|Proteomes:UP000245021};
RA   Noda S., Aihara C., Yuki M., Ohkuma M.;
RT   "Draft Genome Sequence of Lactococcus sp. Strain NtB2 (JCM 32569), Isolated
RT   from the Gut of the Higher Termite Nasutitermes takasagoensis.";
RL   Genome Announc. 6:e00445-18(2018).
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:GBG96491.1}.
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DR   EMBL; BFFO01000003; GBG96491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R5HJL8; -.
DR   Proteomes; UP000245021; 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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245021};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..273
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          374..642
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  82901 MW;  B9C7F24B3A43CD28 CRC64;
     MTEEQERLTR RRKKATGDQS KTAKKETIIN KESNPVKYYA SKVWRPFRRF WKKYSLTKVS
     LIALIVLVVA TGSYLFYLAK SANVSVLQSS ISAQTEIIDK NGNVAGELYG SKGSSVEFNQ
     ISDNVKNAVV ATEDRTFYKN HGVNLGRFIL ATVTLGRFGG GSTITQQLAK NAYLTQAQTI
     DRKAREFFLA LEINKHYSKQ QILTMYLNNS YFGNGVWGIQ DASEKYFGIP ASDLTVDEAA
     TLAGMLKGPE IYNPLYKNAQ YAVPRRNTVL QNMVNAGFLK QDEADGYAKV DLLSELKDNY
     VPQTKSYKYP SYFNAVITEA ENKFGMTLQE IMNNGYKIYT SLDSNMQTGM QATYSNVSLF
     PQAADGTYAQ SGSVAIDPKT GGVSALVGNV DTGDYNAFLN FNYATQSKRS TGSTIKPLIA
     YLPAVQSGWS TDKVLSDVGK NFGSSSNPYE PKDDDGMTGH TGQYDGTNYA SGTLPMYQAL
     ANSYNIPALN TYQSIGPEKG NELGKTFGLN LTDKNNILPT VLGSGVETNP WQMAQAYATF
     ANGGVMNTAH IINKVENAAG QTIHKAKVSQ TRVMSESDAD KMTSMMQGTF TNGSAWNAAP
     SSYAMAGKTG TNNTTDQWVI GYTPDIAIAL WVGFPQESNA QYQLEGTSSG QTSVIFRDEA
     SYILPYTPGT KFNSENAYAA HGISPLAADW TQTRQNQDNI VATEQYKNNT TGNAPVQSSG
     SNSSDSSSND SKLGEKIKKG LNDVGNAAKD LWDKASNIFN
//
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