ID Q8E1Q5_STRA5 Unreviewed; 750 AA.
AC Q8E1Q5;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 104.
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:AAM99205.1};
GN OrderedLocusNames=SAG0298 {ECO:0000313|EMBL:AAM99205.1};
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435 {ECO:0000313|EMBL:AAM99205.1, ECO:0000313|Proteomes:UP000000821};
RN [1] {ECO:0000313|EMBL:AAM99205.1, ECO:0000313|Proteomes:UP000000821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821};
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin S., Kolonay J.F., Umayam L.A., Madupu R., Lewis M.R.,
RA Radune D., Fedorova N.B., Scanlan D., Khouri H., Mulligan S., Carty H.A.,
RA Cline R.T., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C.,
RA Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R.,
RA Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAM99205.1; -; Genomic_DNA.
DR RefSeq; NP_687333.1; NC_004116.1.
DR RefSeq; WP_000628368.1; NC_004116.1.
DR AlphaFoldDB; Q8E1Q5; -.
DR STRING; 208435.SAG0298; -.
DR KEGG; sag:SAG0298; -.
DR PATRIC; fig|208435.3.peg.296; -.
DR HOGENOM; CLU_006354_2_5_9; -.
DR OMA; LAQMAMI; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000000821; Chromosome.
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/1B; 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:UP000000821};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..239
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 335..628
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 678..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 82573 MW; 80A29580608B2031 CRC64;
MITIKKESVI KLLKYAFGII MGFIILAIVI GGLLFAYYVS RSPKLTDQAL KSVNSSLVYD
GNNKLIADLG SEKRESVSAD SIPLNLVNAI TSIEDKRFFK HRGVDIYRIL GAAWHNLVSS
NTQGGSTLDQ QLIKLAYFST NKSDQTLKRK SQEVWLALQM ERKYTKEEIL TFYINKVYMG
NGNYGMRTTA KSYFGKDLKE LSIAQLALLA GIPQAPTQYD PYKNPESAQT RRNTVLQQMY
QDKNISKKEY DQAVATPVTD GLKELKQKST YPKYMDNYLK QVISEVKQKT GKDIFTAGLK
VYTNINTDAQ KQLYDIYNSD TYIAYPNNEL QIASTIMDAT NGKVIAQLGG RHQNENISFG
TNQSVLTDRD WGSTMKPISA YAPAIDSGVY NSTGQSLNDS VYYWPGTSTQ LYDWDRQYMG
WMSMQTAIQQ SRNVPAVRAL EAAGLDEAKS FLEKLGIYYP EMNYSNAISS NNSSSDAKYG
ASSEKMAAAY SAFANGGTYY KPQYVNKIEF SDGTNDTYAA SGSRAMKETT AYMMTDMLKT
VLTFGTGTKA AIPGVAQAGK TGTSNYTEDE LAKIEATTGI YNSAVGTMAP DENFVGYTSK
YTMAIWTGYK NRLTPLYGSQ LDIATEVYRA MMSYLTGGYS ADWTMPEGLY RSGSYLYING
TTTTGTYSSS VYKNIYQNSG QSSQSSSSTS SEKQKEDKNT ANDANSSSPQ VETPNNGNAT
TPNNSNQTVP GTGHGNGNGN GNNNTVPNGN
//