ID A0A1G7DFK3_9FLAO Unreviewed; 786 AA.
AC A0A1G7DFK3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05421855_101952 {ECO:0000313|EMBL:SDE50293.1};
OS Ulvibacter litoralis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacter.
OX NCBI_TaxID=227084 {ECO:0000313|EMBL:SDE50293.1, ECO:0000313|Proteomes:UP000199321};
RN [1] {ECO:0000313|EMBL:SDE50293.1, ECO:0000313|Proteomes:UP000199321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16195 {ECO:0000313|EMBL:SDE50293.1,
RC ECO:0000313|Proteomes:UP000199321};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNBA01000001; SDE50293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7DFK3; -.
DR STRING; 227084.SAMN05421855_101952; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000199321; 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:InterPro.
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 4: Predicted;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199321}.
FT DOMAIN 62..221
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 301..572
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 690..779
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 786 AA; 88452 MW; F096A695CB4C38A5 CRC64;
MKKTSATFFK KHKLKLSFGG ILFAIWLFCL PSELFQVPTA TVVESSEGVM LGARIADDGQ
WRFPKMDSVP YRFEQSILLF EDEYFYRHPG FNPISISKAL WQNMTTNKRR GGSTLTQQVI
RISRKNKQRN YAEKLIEIMQ ATRLEAGYSK EEILGFYASY APFGGNVVGL ETASWRYFGI
PASELSWGQS AALAVLPNAP SLIFPGKNEA ILKEKRDRLL LKLFQKGKID QTTYNLALDE
HLPGKPFPLP EIAPHLTEKI RKEHRGKRVE TTVLYSLQKK INNITKTHHK QLRQNQINNL
AVLVLDVNTR EVLAYVGNAP TTRENNNYVD IIAKSRSTGS VLKPFLFSAL LSSGELLPNT
LIADIPTVVN GYSPENFDKQ FHGAVPASEA LSRSLNIPAV RMLQSYGLDR FYNRLQELNF
SQIKKPANHY GLTLILGGAE SSLWDITKAY AGMASTLNYF NRSSSEYRAT EFIEPIYING
ETGDFGTVKN VAPIFNAGAI YNTLEALQKV NRPTGEENWS FFSNSQPIAW KTGTSYGFKD
AWAVGVTPKY AIGVWVGNAD GEGRPGLTGV QAAAPILFDV LDALPKSEWF DVPYDELIEA
NVCKKSGYLA GVFCEDVASE WIPKEGTKTS SCPYHQTVFL NASEKKRVNS SCYPLSEMKQ
KSWFTLPPVL EYYYAPLHPE YITLPSFASE CLQEGERKME FIFPKKNETI LLPKTFDENV
NDVVFKLAHR TPETTVFWYL DTTFMGSTET FHEITFAPKP GIYLLTATDE EGNEVKQQVE
ILQASK
//
