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Database: UniProt
Entry: G4AAI9_AGGAC
LinkDB: G4AAI9_AGGAC
Original site: G4AAI9_AGGAC 
ID   G4AAI9_AGGAC            Unreviewed;       785 AA.
AC   G4AAI9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SC1083_1862 {ECO:0000313|EMBL:EGY32846.1};
OS   Aggregatibacter actinomycetemcomitans serotype e str. SC1083.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=907488 {ECO:0000313|EMBL:EGY32846.1, ECO:0000313|Proteomes:UP000005508};
RN   [1] {ECO:0000313|EMBL:EGY32846.1, ECO:0000313|Proteomes:UP000005508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC1083 {ECO:0000313|EMBL:EGY32846.1,
RC   ECO:0000313|Proteomes:UP000005508};
RA   Chen C., Kittichotirat W., Asikainen S., Bumgarner R.;
RL   Submitted (OCT-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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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:EGY32846.1}.
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DR   EMBL; AEJM01000037; EGY32846.1; -; Genomic_DNA.
DR   RefSeq; WP_005558909.1; NZ_AEJM01000037.1.
DR   AlphaFoldDB; G4AAI9; -.
DR   SMR; G4AAI9; -.
DR   PATRIC; fig|907488.3.peg.1832; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000005508; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR011815; PBP_1c.
DR   InterPro; IPR009647; PBP_C.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; TIGR02073; PBP_1c; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR   Pfam; PF06832; BiPBP_C; 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   3: Inferred from homology;
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}.
FT   DOMAIN          53..210
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          310..556
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          694..778
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   785 AA;  88737 MW;  05189A89EDF2DC4A CRC64;
     MSQISRKSLY FVLCGLLLTC IGGRFLPHIP LKQRFPYSIA VYDEQQNLLR LTTAKDQKYR
     LWTPLEELSP QLVDAVLFQE DEWFYYHFGV NPYGLLRGAT QTYLFGGSPQ GGSTITMQLA
     RILWKIDSRT IGGKIEQILR AIQLELQYSK REILEAYFNF APYGRNIEGA GTASLIYFNR
     ASKNLNLAEA MTLAILPKNP NAYIQQNNQQ LNAQLFNARN KLYARWVESH PKDRQWQSHF
     KLNYPLRPLE KLPFFAPHFT DQVLQQYAES EAIQNGRIVT GLNSGLQRLV ERISLRYLQQ
     QKPYGVNNLA VLLVNNRTMQ IKALVGSGDY FNQHISGQIN GTLAKRSYGS TLKPFIYGLA
     FDQGLVHPKT ILKDLPTTFA DYQPENYEGN FLGPVSVTQA LLQSRNIPAV DMAQRLKYPD
     LYDLLKQAKI TLPKEKAHYG LSLVLGGAEL SMQQLAGLYA ALANGGQWRP LHTLKSALAT
     QSATLLSPES SYMLGDILSQ NIRTDIYNKA IKTKLPIYWK TGTSNGLRDA WTAGYFGNYT
     LVVWLGNFNN KSNPHFIGRR LAAPLFLQLA DGIIAQYPNM KNPLSRDKLK LTEVPVCAAD
     GNLPNKYCQQ LTKTFFIPGK SPIQVSNTYQ QLRVRKGTDV LACATDPNAQ TEQKIYEIWG
     SDYQKMFAQA GIIKRNPIVN VECPYEQQNQ SLQQITHNPL KMTSPLENRT YYINMNSPEN
     HIPLTATTSG EVQHLYWFVN NVYLGESPAS KAFLWQPAKS GTYQITVADE QGHRTGVSVV
     VSVVR
//
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