ID A0A3S3QNL7_9FLAO Unreviewed; 802 AA.
AC A0A3S3QNL7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpC {ECO:0000313|EMBL:RWW93786.1};
GN ORFNames=EPI11_14730 {ECO:0000313|EMBL:RWW93786.1};
OS Flavobacterium cerinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2502784 {ECO:0000313|EMBL:RWW93786.1, ECO:0000313|Proteomes:UP000287527};
RN [1] {ECO:0000313|EMBL:RWW93786.1, ECO:0000313|Proteomes:UP000287527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1E403 {ECO:0000313|EMBL:RWW93786.1,
RC ECO:0000313|Proteomes:UP000287527};
RA Zhang R., Du Z.-J.;
RT "Flavobacterium sp. nov.,isolated from freshwater.";
RL Submitted (JAN-2019) 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 -!- 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:RWW93786.1}.
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DR EMBL; SBII01000011; RWW93786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3QNL7; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000287527; 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:UP000287527}.
FT DOMAIN 80..242
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 320..564
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 708..796
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 802 AA; 90914 MW; 6DC2EDC3FD538659 CRC64;
MKNKFRAFLK NTYRVFKTLL ERIFHWIKAN KIKSAIALLL LIGYYFCLPR TLFSEPYSTV
IESSEGELLG ARIARDGQWR FPEQDSVPYK FRECIVHFED QHFYSHPGFN PVAIVNAVRQ
NYKAGKVVRG GSTLTQQVIR LSREGKKRSY FEKFIEMVLA TRLEFRHSKD AILGLYAAHA
PYGGNVVGLE MASWRYFGVQ PHQLSWAETA TLAVLPNAPS LIYPGKNQQH LLAKRNRLLK
KLFEEKIIDQ TTYELSLQED LPNKPFNLPQ AAPHLLQNIA KTKEGQRIKT TVKNGLQARV
NQIAARYYQD YKQTEVHNLA ILVIDVQTRN IVAYVGNSPT DMAHQKDVDI IPAPRSTGSI
LKPFLFAAML DAGEILPNTL VADVPTQIAG YSPKNYELTY DGAVPAQRAL SRSLNIPSVL
MLKEYGVYRF YDQLKHFKLR DINKHPNHYG LSLILGGAES NLWDLCRTYA GLSGTLNYFN
AHQAKYRTGE FAELNWDHDH ENDYGKDIFN KPQLGAGSIW LTYNAMKEVN RPQGDEAWRF
YDSSLEIAWK TGTSFGGRDG WAIGTSSKYV VGVWVGNASG EGRPSLTGVG SAAPILFDVF
NLLPRTKWFA APFNDLEEAD VCALSGHLAG DHCPVVKQWI PLSRSKTSMC PYHKTIHLDP
TGQYQVNSSC ESVDNMITKT WFVLPPVMEW YYKSLHMDYM PLPPFRADCQ GVTSGSMDFI
YPKETGKIYL AKDFNGVIQP FVLKAAHSSP NAKLFWYLGD KYLGETKTFH EMQVEAKTGK
YILTVTDESG NEIRRKIEIV SE
//
