ID A0A1G9EWK0_9BACT Unreviewed; 812 AA.
AC A0A1G9EWK0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN05421823_103606 {ECO:0000313|EMBL:SDK80489.1};
OS Catalinimonas alkaloidigena.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Catalimonadaceae;
OC Catalinimonas.
OX NCBI_TaxID=1075417 {ECO:0000313|EMBL:SDK80489.1, ECO:0000313|Proteomes:UP000198510};
RN [1] {ECO:0000313|EMBL:SDK80489.1, ECO:0000313|Proteomes:UP000198510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25186 {ECO:0000313|EMBL:SDK80489.1,
RC ECO:0000313|Proteomes:UP000198510};
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};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; FNFO01000003; SDK80489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9EWK0; -.
DR STRING; 1075417.SAMN05421823_103606; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000198510; 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: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; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 Reference proteome {ECO:0000313|Proteomes:UP000198510};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..267
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 441..685
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 812 AA; 90906 MW; 1AF0ABBBA4F2D647 CRC64;
MQLILSQADA LAKRVAAYFQ HTFQRKSIRI LWVSAAVALV LPLVFLWAIE INALHLFGPM
PGMAKLENPK IAVPSYVFTS DGQLLGKYFR ENRSPVEFSD LPPHLIEALL ATEDIRYREH
SGIDPEALGS VVYYSLKGKN RGGSTITQQL TKNLYRTRGE EEQGYLSSVS GLGTLIYKLK
EWILSVKIER AYTKEEILTM YLNTVAFGSE AYGVKTAAKT YFSKSLDSLT VEEAATLVGL
LKATTTYNPL IHPDRSRERR NVVLAQMAKY GYLSAAEADS LQALPLVVEP TLERVADGPS
GYYRHALQQN LEAWCEENGY DLYTDGLMIY TTLDSRVQAH AEAAVKKRMS QLQGVFNEHW
RGQNPWIDGR KREIPNFIEQ AAQRTKTYKY LAESLKGDSV AIWRAMNEPH PMRIFTWNGE
VDTTLSTLDS LRYYKKLLHT GFMAMDPYNG HIKAWVGGID YGHFQYDHVQ QAKRQPGSTF
KPFVYAAALE EGYSPCDRFV DQPVTVRYLE NGEKKAWSPR NADWVFSGRS MSLRWAMAKS
VNSITAQLTE KIGWDTVADY ARRMGIDSPL EEVPSIGLGS SDVSVYEMVG AYGTFVNGGV
WTQPILLARI EDRHGNLIHE FVAPRRRAIS EETAYLMTYM LRGTLEEPEG TAQGLWAYDV
HRGNQIGGKT GTSSNYSDGW FISVTKDLIA GTWVGAEDRS VHFRTSSLGE GGKTALPLVG
EFLEQVYDDD SLGYAFGKFN KPEAEIKKQY QCPTIIPEPI DIAIDSVVIE AKRVQPLPLG
PTQAKAEPAL PVVGGIRSIV QTEGNRAVRN QE
//
