ID A0A125BCW5_THIDE Unreviewed; 1071 AA.
AC A0A125BCW5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ABW22_07515 {ECO:0000313|EMBL:KVW96782.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW96782.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW96782.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW96782.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(2015).
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}.
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:KVW96782.1}.
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DR EMBL; LDUG01000019; KVW96782.1; -; Genomic_DNA.
DR RefSeq; WP_059754205.1; NZ_LDUG01000019.1.
DR AlphaFoldDB; A0A125BCW5; -.
DR STRING; 1123392.GCA_000376425_02095; -.
DR PATRIC; fig|36861.3.peg.980; -.
DR OrthoDB; 8552189at2; -.
DR Proteomes; UP000064243; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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; IPR036950; PBP_transglycosylase.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 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 Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000313|EMBL:KVW96782.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW Transmembrane {ECO:0000313|EMBL:KVW96782.1}.
FT DOMAIN 136..320
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT REGION 1011..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 118290 MW; B06E1B3EC4654FFB CRC64;
MHKVPRRILI GLVVLLLIVG LVGLIAWELL SSALEAKYLT KTAQKMTWQI QPGPSGRIRY
PGEGPYDVRL GYSKLPDYLA RLDQAGWQID RQAKISSQMA RAADLGLFLP YHEKDQAGLS
LLDSDGQPLY QAKYPSWGYG RFEDIPDVLV NALLYIENRE LLTEQFPTRN PAVEWDRLAQ
ALIEKGISLV DTNRNVPGGS TLPTQIEKYR HSPDGLTASM SEKLRQMGTA SLRAYLDGPN
TLSMRREIVT AYLNTVPLAA APRYGEVNGI GDGLWAWYGL DFDEVNRTLA KPPRSKDAAY
ASMLKHALSL IVAERRPSYY LAANRKALDA LTDDHLDLLA NAELIPRELA DQAKQVELRT
TRHRVDPPPP RFVDQKAANA LRIRVSALLG ESRLYDLDRL DLQIDTNINQ PAQKIVSTYL
QSLAKPQAAA ASGLIGHRLL QPGNPLGEVI YSFTLYEKTA QGNLLRIQAD NLNQPFDINS
QARLDLGSTA KLRTLVTYLE IIARLHADYH VLDAAMLRQK AQPQRDVLAQ WVAASLLSQP
GIRLDALLEA AMRRPYSAAL ETFFTGGGLH NFVNFDPKDN DRVMDVWEAT KNSVNLVYIR
IMRDIVRHYA SSTPGAGGRI LDDASNPMRE TYLARFVDQE GRVFTNRFYQ RHKALTPEQM
AEDLYTRIGH NPRRFSAVFR YLEPQAKLEA YVDALRAHVP ASASLSQKTL KSLYQTYAPE
AYSLTDRGYI AQIHPLELWV VKTLRGTPGT DLKTLYESGT GVRLEVYEWL FKTSRKNAQD
IRIQSFLEVE AFESLLADWK RLGYPFDNIT PSYATAIGSS GDRPAALAEL MGILVNDGVR
APMVSLTGLH FAANTPYDTR LSMKPPKGER LMPAEVARTV RSALANVVKS GTAVRLAGAL
KDSAGQPLIL GGKTGTGDHR FERFGRGGQR LESRVVNRTA TFVFYLGDRH FGTLTALVQG
EQAGQFGFTS SLTAQMLKTL LPQLQPHLDL QPPAPPKVAA DAVAEPAAVV APAPRAPAQE
KPDGSTSQAD PPVKQPAPFQ GGFPEDLEPS VVVPVPVIPA TPPPPDGAPE P
//
