ID E0Q4A3_9STRE Unreviewed; 731 AA.
AC E0Q4A3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbp2A {ECO:0000313|EMBL:EFM34424.1};
GN ORFNames=HMPREF9189_1884 {ECO:0000313|EMBL:EFM34424.1};
OS Streptococcus sp. oral taxon 071 str. 73H25AP.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=864570 {ECO:0000313|EMBL:EFM34424.1, ECO:0000313|Proteomes:UP000005184};
RN [1] {ECO:0000313|EMBL:EFM34424.1, ECO:0000313|Proteomes:UP000005184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73H25AP {ECO:0000313|EMBL:EFM34424.1,
RC ECO:0000313|Proteomes:UP000005184};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (AUG-2010) 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:EFM34424.1}.
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DR EMBL; AEEP01000017; EFM34424.1; -; Genomic_DNA.
DR RefSeq; WP_000762591.1; NZ_GL397254.1.
DR AlphaFoldDB; E0Q4A3; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_2_9; -.
DR Proteomes; UP000005184; 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; 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 NCBIfam; NF038276; strep_PBP2A; 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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..270
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 371..630
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 731 AA; 80557 MW; 67EEF0802CB6C9EF CRC64;
MKLDKLFEKF LSLFKKETNE SAESDSTSMR RSRSDRKKLS QVGAIRKFWR RYHLTKIVII
LGLSAGLLVG TYLFAIAKST NVNDLQNALK TRTLIFDREE KEAGALSGQK GTYVELADIS
KDLQNAVVAT EDRSFYKNDG INYGRFFLAI LTAGRSGGGS TITQQLAKNA YLSQDQTVER
KAKEFFLALE LTKKYSKEQI LTMYLNNAYF GNGVWGVEDA SKKYFGVSAS QLTLDQAATL
AGMLKGPELY NPLNSVETST NRRDTVLQNM VAAGYIDKNQ ETEAAGTDMA SQLQDKYEGK
VSDYRYPSYF DAVVNEAVSK YNLTEEEIVN NGYRIYTELD QNYQANMQVV YENTSLFPKA
EDGTHAESGS VALEPKTGGV RSVVGHVAGD DKPGFRNFNY ATQSKRSPGS TIKPLVVYTP
AVEAGWALNK QLDNHTMQYD SYQVDNYAGI KTSPEVPMYQ ALAESLNLPA VATVNALGID
KAFDAGERFG LNMENVDRVL GVALGGGVET NPLQMAQAYA AFANEGLMPE AHFITRIENA
SGQVIKSHKN SQKRVIDKSV ADKMTSMMLG TFTNGTGISS SPTDYVMAGK TGTTEAAFNS
VYTSDQWVIG YTPDVVITHW LGFPTTDENH YLAGSTSNGA AHVFRSMANT ILPYTPGSTF
TVENAYKQNG IEPENTKKQA IENEANQSED PIADIRSRAQ NLVDEAGRAI SEAKIKEKAQ
TIWDSFLNLF R
//
