ID A0A1H7LC45_9SPHI Unreviewed; 797 AA.
AC A0A1H7LC45;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05421740_103115 {ECO:0000313|EMBL:SEK96448.1};
OS Parapedobacter koreensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=332977 {ECO:0000313|EMBL:SEK96448.1, ECO:0000313|Proteomes:UP000198916};
RN [1] {ECO:0000313|EMBL:SEK96448.1, ECO:0000313|Proteomes:UP000198916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip14 {ECO:0000313|EMBL:SEK96448.1,
RC ECO:0000313|Proteomes:UP000198916};
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; FNZR01000003; SEK96448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7LC45; -.
DR STRING; 332977.SAMN05421740_103115; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000198916; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..228
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 311..589
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 708..792
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 797 AA; 88629 MW; C4986ACB9642AC8F CRC64;
MDIRIKDFIA FCKSPKGIFI LAFASTLSLV FYFALPKPLF RSPTSFVIED EAGRLLGASI
ALDGQWRFPA TDAVPEKFAK CIVAFEDRRF YIHPGVDPVA LVRAIWQNIR GRRVVSGGST
ISMQVIRMSQ NKPRTIWQKC MEAVLAFRLE AGYNKATILQ LYSAHAPFGS NVVGLDAASW
RYFGRAPEQL SWAEAATLAV LPNAPSLIHP GRNRKRLLAK RNMLLDKLAV QGTLDRSAAE
LAKLEPLPDE PLPLPRLAPH LLERFKKEYG RLGTGVTRLK TSINANLQQR VADIIDRHHR
GLSANGIFNA AALVLEVESG KTMAYVGNVH TPQNAEAESH VDMITALRSP GSTLKPLLYA
AMLTDGLILP HTLIPDIPTQ IGGYTPQNYD LGYDGALPAS RALSRSLNIP AVKMLQHYKY
QRFQPFLRQA GVRTLDRPAD FYGLSMILGG CEVTMWQLAG TYASMARTLN HYRRYHAGYN
STDYRPPHYS RNVGTLPENS VERTSIIDHA SLYFTFQAMN EVMRPGEEAL WEQFASSKKI
AWKTGTSFGF RDGWAIGLTP THVVCVWVGN ADGEGRPGLT GIETAAPILF EIFDLLPARA
WFEAPLDRMV QTAVCRESGH LAGPDCPHPD TVYIPVPGHR SSVCPYHQLI HTNSKGTLQV
TADCAAAGDI VAAQWFVLPP AMEFYYKPRH ATYRELPPFG NGCAIGTDGQ PMEMIYPKNN
AKIYIPLEID GRRGQVIFNA AHRRKGSRIY WHLDETFVGE TETFHQLALD VPAGLHRITL
VDSDGARISQ QFEILKK
//