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Database: UniProt
Entry: B9DV64_STRU0
LinkDB: B9DV64_STRU0
Original site: B9DV64_STRU0 
ID   B9DV64_STRU0            Unreviewed;       739 AA.
AC   B9DV64;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
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:CAR43047.1};
GN   OrderedLocusNames=SUB1407 {ECO:0000313|EMBL:CAR43047.1};
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR43047.1, ECO:0000313|Proteomes:UP000000449};
RN   [1] {ECO:0000313|Proteomes:UP000000449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(2009).
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; AM946015; CAR43047.1; -; Genomic_DNA.
DR   RefSeq; WP_015911727.1; NC_012004.1.
DR   AlphaFoldDB; B9DV64; -.
DR   STRING; 218495.SUB1407; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   KEGG; sub:SUB1407; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_5_9; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000000449; 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   Reference proteome {ECO:0000313|Proteomes:UP000000449};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..40
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..631
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          684..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   739 AA;  81126 MW;  06F5BEAC130737EE CRC64;
     MITIKNPTVQ KWLKYALAAI LSLVIFTIII GGLLFLFYVA TAPKLSETEL KSTNSSLVYD
     ANNELIADLG SEKRENVTAD SIPLNLVNAI TSIEDKRFFN HRGVDLYRIL GAAWHNLTSN
     STQGGSTLDQ QLIKLAYFST KESDQTLKRK AQEVWLALQM ERKYTKQEIL TFYINKVYMG
     NGNYGMLTAS KSYFGKDLKD LSFAQLALLA GIPQAPSQYD PYTQPDSATK RRNVVLQQML
     SEKNISKADY DAAIATPVTD GLQPLKQTSS YPKSMDNYLK QVIAQVKSET NKDIFTAGLK
     VYTNILPDVQ QRLYDIYNTE DYVYYPDDQM QVASTIVDVT NGHVIAQLGG RHLDENVSFG
     TNQAVLTDRD WGSTMKPISA YGPAIESGSY NSTAQSTNDS IYYWPGTTTQ LYNWDRKYNG
     WMTIQTAIMQ SRNVPAVRAL EAASLDYAKS FLSDLGINYP QMHYSNAISS NTTSSEQKYG
     ASSEKMAAAY AAFSNGGIYY KPQYVNKIEF NDGTTKVFEN KGKRAMKETT AYMMTDMLKT
     VLTYGTGTAA QIPGVAQAGK TGTSNYTDDE LVQIGNTLGL YTDYVGTMAP DENFVGYTNK
     YAMSVWTGYK NRLTPVYGDG LLVASKVYKN MMTYLTNGYS EDWIMPSGLY RSGGMLYLSG
     GTYTSGYTNS SVYNNIYSGN SSSASLSNDT SASSSDETSS ASSDASSSAT GGNGNTNGNS
     NSNSTPANNG NGNGNNKIN
//
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