ID I1ZJL5_STRPA Unreviewed; 705 AA.
AC I1ZJL5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbp1A {ECO:0000313|EMBL:AFJ25239.1};
GN ORFNames=Spaf_0214 {ECO:0000313|EMBL:AFJ25239.1};
OS Streptococcus parasanguinis FW213.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1114965 {ECO:0000313|EMBL:AFJ25239.1, ECO:0000313|Proteomes:UP000002865};
RN [1] {ECO:0000313|EMBL:AFJ25239.1, ECO:0000313|Proteomes:UP000002865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW213 {ECO:0000313|EMBL:AFJ25239.1,
RC ECO:0000313|Proteomes:UP000002865};
RX PubMed=22529932; DOI=10.1371/journal.pone.0034769;
RA Geng J., Chiu C.H., Tang P., Chen Y., Shieh H.R., Hu S., Chen Y.Y.;
RT "Complete Genome and Transcriptomes of Streptococcus parasanguinis FW213:
RT Phylogenic Relations and Potential Virulence Mechanisms.";
RL PLoS ONE 7:E34769-E34769(2012).
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; CP003122; AFJ25239.1; -; Genomic_DNA.
DR RefSeq; WP_014712731.1; NC_017905.1.
DR AlphaFoldDB; I1ZJL5; -.
DR STRING; 1114965.Spaf_0214; -.
DR PaxDb; 1114965-Spaf_0214; -.
DR KEGG; scf:Spaf_0214; -.
DR PATRIC; fig|1114965.3.peg.208; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_5_9; -.
DR Proteomes; UP000002865; Chromosome.
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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..235
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 331..624
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 664..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 78262 MW; 7F09A82A67644242 CRC64;
MNKQTVIQWL KYVAIAAISF FLLLFVLGGL IFGYYAMKAP TLSEKDLVAT TSSKIYDNQN
NLIADLGSEK RINVSTNEIP TDLVNAIVAI EDHRFFNHRG VDIIRIGGSF LHNLRGGSQG
GSTLTQQLIK LTYFSTSASD RTLSRKIQEA WLATQLEKKA TKQEILTYYV NKVFMANGNY
GMQTAAKSYY GKDLKDLSLP QLALLAGMPQ APNQYDPYSH PEAAQQRRNL VLKEMLEMKT
ISNKQYEAAV NTPITDGLQS LSSSSSYPAY MDNYLKEVIE QVEEETGYNL LTTGMDVYTN
VDTEAQKKLW DIYNTDEYVN YPDDELQVAS TVIDVNTGKV IAQLGSRHQS SNVSFGTNQA
VETNRDWGST MKPISDYAPA LEHEEYTSTA ATITDAPYNF PHSSTPVYNW DRSYYGSITM
TYAIQQSRNV PAVKALEKVG LKKAKKFLNG LGIDYPEMVY ANAISSNTSD SSNKYGASSE
KMAAAYAAFA NGGTYYKPSY VNRVVFSDGT TKEFDSEGTR AMKATTAYMM TDMMKTVLMS
GTGTNAAISG VYQAGKTGTS NYSDNELSKL TKNSSYSSIV APDELFVGYT PEYSMAVWTG
YSNRLTPVLD NGMQVATDVY RQMMLYLANN NNSGHTDWTQ PSGLYRNGSY LYLNNGKNNY
NNYYYEPSYS TEESSTEESS SSSSSEENPS KPTEPSSQDS NNHNE
//
