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
//