ID W8ETK9_9BACT Unreviewed; 778 AA.
AC W8ETK9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=Hsw_0278 {ECO:0000313|EMBL:AHJ95873.1};
OS Hymenobacter swuensis DY53.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ95873.1, ECO:0000313|Proteomes:UP000019423};
RN [1] {ECO:0000313|EMBL:AHJ95873.1, ECO:0000313|Proteomes:UP000019423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY53 {ECO:0000313|EMBL:AHJ95873.1,
RC ECO:0000313|Proteomes:UP000019423};
RA Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT "Complete genome sequence of ionizing-radiation resistance bacterium
RT Hymenobacter swuensis DY53.";
RL Submitted (JAN-2014) 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; CP007145; AHJ95873.1; -; Genomic_DNA.
DR AlphaFoldDB; W8ETK9; -.
DR STRING; 1227739.Hsw_0278; -.
DR KEGG; hsw:Hsw_0278; -.
DR PATRIC; fig|1227739.3.peg.547; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_10; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000019423; Chromosome.
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 ECO:0000313|EMBL:AHJ95873.1}; 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:UP000019423};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..263
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 439..680
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 778 AA; 87878 MW; 1706359C7139BABE CRC64;
MARSATKNSI RKTTPTGRYT GWARTFWLLF GAGAAGLVLY VLAVSVNFLN LFGRMPNLKT
LENPRSELAS EIYSTDNVLM GKYFRENRTP AEYEDLPQHL VDALIATEDA RFEEHSGIDP
KATGRVAAGL LTGGSGGGGS TLTQQLAKVL FRTREDLNDG TLNDVPGVRM LVTKTKEWIL
ATRLERSYTK REILRMYLNT NDYGSNAFGI NTAAKTFFSK KPRELTRPEA ATLVGVLNAP
TRFSPKFNPE RSRVRRNWVL RQMNKYGYIT PQQLQADTLK PIVLRYSVEN QNEGIAPYFR
VEVSKMLKQW AKETDHDLYA DGLKIYTTID SRMQKYAEAA VAEHMKLQQK WFDQQWKGQQ
PWRDENGRII PNFLSTSIKR TERYRSLTTR FEGNKDSIKY YLNRKYKMKV FTWNGGEKEV
LMSPMDSLAY YKRLLHSGFM AMNPLNGQVK AWVGGINFKY IKYDHVKQGK RQPGSTFKPF
VYVAAIDQGY SPCYQRPDVA TTFPAERGRP AYTPRNFEGS YSGRTFTLRQ ALARSMNSIT
AWLVQKLGPE TVVSYAKRLG ITSPIEAVPA VGFGSSDVSI YELAGAYSTF VNKGIWTAPM
MVTRIEDKNG NVLREFVPQT REALSEETAY LMTYMLRGAT EEKGGTSIIL KGGFKFPYEM
GAKTGTTSNY SDGWFMGLTP DLVCGMWVGG EDRSIHFKTG AYGQGSRMAL PLYGIFMKKV
YADKSVDINT GPFPKPAQAL SIEIDCSRYY NGSGQRDTIP SDQKLNQVEL EDLNEEDI
//
