ID A0A2X3VDP5_9STRE Unreviewed; 741 AA.
AC A0A2X3VDP5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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 Name=ponA_2 {ECO:0000313|EMBL:SQF39574.1};
GN ORFNames=NCTC12278_00428 {ECO:0000313|EMBL:SQF39574.1};
OS Streptococcus ferus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1345 {ECO:0000313|EMBL:SQF39574.1, ECO:0000313|Proteomes:UP000249495};
RN [1] {ECO:0000313|EMBL:SQF39574.1, ECO:0000313|Proteomes:UP000249495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12278 {ECO:0000313|EMBL:SQF39574.1,
RC ECO:0000313|Proteomes:UP000249495};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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 ---------------------------------------------------------------------------
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; LS483343; SQF39574.1; -; Genomic_DNA.
DR RefSeq; WP_018030920.1; NZ_LS483343.1.
DR AlphaFoldDB; A0A2X3VDP5; -.
DR STRING; 1123303.GCA_000372425_01607; -.
DR KEGG; sfer:NCTC12278_00428; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000249495; Chromosome 1.
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:UP000249495};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 344..614
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 683..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 81730 MW; 82E524FEC5210254 CRC64;
MTIKFDQLKN IKFDKKFFLT VLKYLAGALA SLVILAVVVG GLLFAYYVSS TPKLSESKLK
ATNSSLVYDS SNNLIADLGA EKRESVSSDN VPLNLVNAIT SIEDHRFFKH RGVDIYRIIG
AAWKNAFSDS TQGGSTLDQQ LIKLAYFSTK KSDQTLKRKA QEAWLALQME RKYTKEEILT
FYINKVYMGN GNYGMKTAAK SYFAKDLKDL SIAQLALLAG IPQAPSQYDP YVHPDAAKTR
RDTVLKQMYR YKKISKAEYD EAIQVPITDG LQELKESSSY PKYMDNYLKQ VIAEVKSRTG
QDIFSAGMKV YTNVNADAQQ YLWDIYNSDQ YIAYPDSDFQ VASTVVDVTN GKVIAQLGSR
NQDTNVSFGT NQAVLTDRDW GSTMKPISAY GPAIETGAFT TTAQMLNDSV YYWPGTTTQL
YNWDRRYNGW MTMQTAIQQS RNVPAVRALE AAGLDNAKNY LSGLGIDYPE MNYSNAISSN
NSSSSQKYGA SSEKMAIAFA AFANGGTYYK PQYVNKIEFK DGTTETYDAQ GSRAMKETTA
YMMTDMLKTV LTYGTGTQAQ ISGLYQAGKT GTSNYTDDEL PKISEKYGLN PYSLGTIAPD
ENFVGYTSQY AMAVWTGYKD RLHPVYGDSL NIAAQVYRTM MLHLTGGVST DWTMPDGLYR
SGSYLYLDGS SGSNSKYAGG NYSSTTAATS SDSSDDSSNN NNDSTQASND SSETNNNSSN
QDSNSQTTEA AASSETSDNG E
//
