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Database: UniProt
Entry: B2Y3L9_STREE
LinkDB: B2Y3L9_STREE
Original site: B2Y3L9_STREE 
ID   B2Y3L9_STREE            Unreviewed;       681 AA.
AC   B2Y3L9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE   Flags: Fragment;
GN   Name=pbp1a {ECO:0000313|EMBL:ACB14491.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:ACB14491.1};
RN   [1] {ECO:0000313|EMBL:ACB14491.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=580.1GR00 {ECO:0000313|EMBL:ACB14491.1};
RX   PubMed=18394970; DOI=10.1016/j.meegid.2008.02.001;
RA   Stanhope M.J., Lefebure T., Walsh S.L., Becker J.A., Lang P.,
RA   Pavinski Bitar P.D., Miller L.A., Italia M.J., Amrine-Madsen H.;
RT   "Positive selection in penicillin-binding proteins 1a, 2b, and 2x from
RT   Streptococcus pneumoniae and its correlation with amoxicillin resistance
RT   development.";
RL   Infect. Genet. Evol. 8:331-339(2008).
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};
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DR   EMBL; EU377943; ACB14491.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2Y3L9; -.
DR   GO; GO:0005576; C:extracellular region; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          42..218
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          313..600
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          633..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACB14491.1"
FT   NON_TER         681
FT                   /evidence="ECO:0000313|EMBL:ACB14491.1"
SQ   SEQUENCE   681 AA;  75337 MW;  C6231699E399946C CRC64;
     LVIAAIVLGG GVFFYYVSKA PSLSESKLVA TTSSKIYDNK NQLIADLGSE RRVNAQANDI
     PTDLVKAIVS IEDHRFFDHR GIDTIRILGA FLRNLQSNSL QGGSTLTQQL IKLTYFSTST
     SDQTISRKAQ EAWLAIQLEQ KATKQEILTY YINKVYMSNG NYGMQTAAQN YYGKDLNNLS
     LPQLALLAGM PQAPNQYDPY SHPEAAQDRR NLVLSEMKNQ GYISAEQYEK AVNTPITDGL
     QSLKSASNYP AYMDNYLKEV INQVEEETGY NLLTTGMDVY TNVDQEAQKH LWDIYNTDEY
     VAYPDDELQV ASTIVDVSNG KVIAQLGARH QSSNVSFGIN QAVETNRDWG STMKPITDYA
     PALEYGVYDS TATIVHDEPY NYPGTDIPVY NWDRGYFGNI TLQYALQQSR NVPAVETLNK
     VGLDRAKAFL NGLGIDYPSI HYANAISSNT IESNKQYGAS SEKMAAAYAA FANGGIYHKP
     MYINKIVFSD GSEKEFSNVG TRAMKETTAY MMTEMMKTVL AYGTGRGAYI PSLPQAGKTG
     TSNYTDDEIE KYIKNTGYVA PDEMFVGYTR KYSMAVWTGY SNRLTPIVGD GFLVAAKVYR
     SMMTYLSEGS NPEDWNIPEG LYRNGEFVFK NGARSTWNSP APQQPPSTES SSSSSDSSTS
     QSSSTTPSTN NSTTTNPNNN T
//
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