ID A0A3L9DJW8_9STRE Unreviewed; 726 AA.
AC A0A3L9DJW8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=EAF07_10030 {ECO:0000313|EMBL:RLY01265.1};
OS Streptococcus hillyeri.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=2282420 {ECO:0000313|EMBL:RLY01265.1, ECO:0000313|Proteomes:UP000279194};
RN [1] {ECO:0000313|EMBL:RLY01265.1, ECO:0000313|Proteomes:UP000279194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28462 {ECO:0000313|EMBL:RLY01265.1,
RC ECO:0000313|Proteomes:UP000279194};
RA Macfadyen A.C., Waller A., Paterson G.K.;
RT "Streptococcus hillyeri sp. nov., isolated from equine tracheal sample.";
RL Submitted (OCT-2018) 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 -!- 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:RLY01265.1}.
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DR EMBL; RCVM01000031; RLY01265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L9DJW8; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000279194; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 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 NCBIfam; NF038272; strep_PBP1A; 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 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:UP000279194};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..252
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 348..645
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 681..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 81137 MW; EBCB406C7A31647C CRC64;
MISIKNARKK LKPSRTKNSS PWKKILGYLT IGLLSIIILA VLAGGGLFAF YASQAPELSQ
EKLQATSSSL IYDKDNNLIA DLGTEKRELV TSDNIPIGLV NAVVSIEDHR FFQHRGIDIY
RILGSVWHNL TNDTTQGGST LDQQLIKLAY FSTAESDRTI KRKIQEIWLA LQMERQFTKE
EILTFYINKV YMGNGNYGMR TAAKSYFGKD LTELSVAQLA LLAGIPQAPS QYDPYTQPEL
ATKRRDIVLS QMYRHDYITK EEYDSAVATP VNDGLQALKP ATSFPKYYDN YLTEVIAEVQ
KQTGLNIFNS GLKVYTNVDS AAQEYLYDIY NTDTYVAYPD EEFQVASTVM DVTNGHVIAQ
LGVRNQQEDI TFGSNQAVLT DRDWGSTMKP ITDYAPAIEN EVYTSTAQNL NDSFYYWPNT
KTQIHNWDRQ YYGWMTMQSA IMQSRNIPAV RALEATGLEK ASHFLAGLGI TYPELYYSNA
ISSSTSSTDQ QYGASSEKMA AAYAAFANGG IYYEPQYVNK ITFSDGSSKT YKAKSNRAMK
ETTAYMMTDM LKTVLYSGTG TSAQIYGVHQ AGKTGTSNYT DDELAAIEKN LGLTNWNVGL
MAPDESFVGY TPQYSMAVWT GYKNRLTPVY GQGLSIANDV YREMMTYLTG GYNKDWTMPD
GLYRSGSYLY LSDATPSYNY YEETTDDSST SESETSESSS VTESSTLDDT GSQTTNTNEI
TSTNRN
//
