ID W4ADH2_9BACL Unreviewed; 1031 AA.
AC W4ADH2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=C161_30316 {ECO:0000313|EMBL:ETT29414.1};
OS Paenibacillus sp. FSL R5-192.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT29414.1, ECO:0000313|Proteomes:UP000019041};
RN [1] {ECO:0000313|EMBL:ETT29414.1, ECO:0000313|Proteomes:UP000019041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT29414.1,
RC ECO:0000313|Proteomes:UP000019041};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT29414.1}.
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DR EMBL; ASPR01000079; ETT29414.1; -; Genomic_DNA.
DR RefSeq; WP_036614680.1; NZ_ASPR01000079.1.
DR AlphaFoldDB; W4ADH2; -.
DR PATRIC; fig|1226754.4.peg.6109; -.
DR Proteomes; UP000019041; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 3.90.1310.40; -; 1.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS50853; FN3; 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 26..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 949..1031
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 324..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 113261 MW; 454BC23A7C04F2CA CRC64;
MVDVNKKKPD EQPVRKRSFA RRLGSFIKWM VVLGFMGALF VGGALMGYVS SIVKDEPVRS
RALIEQKVSE NSITGFAYFA DGSPIGQLRT EEDRRPVTTD QIPQKVIDAV VSIEDNHFYE
HKGVDMSGTL RAVKQKVLKE SVQTGGSTLT QQLARRVFLN LDRTEDRKVK EILLSLRLER
FLTKDEIMTA YLNKVPFGNG SSGYNVYGIK AAAKGLFNIN DLEKINIAQA AYLAGLPQLP
SSYSAFNGKG DFVEENFDRA INRQHLVLRR MLELGKINQS EHDEALAFDI KSALAPKTIK
AYNTYPYLMM ETERQAAQIL MKQLNSDTAE STDKATDADT PQKESSALLE EAQTQLRTGG
YRIYTTINKS IYKTMRTIAE DDSNFSADDP VKGKEQTAAM LINHKTGAIL GMIEGRDFQD
EQMNYATQMV RQPGSTMKPI AAYLPALDEG LVQPASIIDD SPIILKNGPS GYHIAKNANN
RYQGLVTARR ALNYSLNIPA LKLFNEEVGI EKAWTFAKKL GITTIQKEDY QAQTGVLGGL
QYGVTVEELT SAYGAIANKG VYNDSYMISK IVDSKGNIVY KHDTEPVQAF SEQTAYLMTD
MLRTVITEGT ADKVRENYKY SKSVPIVGKT GSTQNYADVW FEGYTPDVTL GVWVGYKQPV
NTLESKSQRK RAQQLWSKIL NEVIDTQKDL FVTDSFKKPS GIETRTVSAY SGKLPTSMTD
KFVTDIFNSK FVPKDSDDGV SKARYITYNG VNYIPRDGTP SDMLKEKTVI KRKKPISDLI
KELQNAFSRM SRHESLAYYL PEDAGADMPT QIDPRTDNGK APDAPGNVRI STSGDRAVIT
FNATPENDVV GYRLYRSVNG GGFQNQGQVV LAGESRSFSA YAAQGGNFAF YVTAVDVAGR
ESAPSATVNS AGVAPPVEEE IDEPIEVPGT VVTPGETQTD NTTTTTPGTP GQVSVSALTQ
GLRIQWAASP NADSYTVYYS ETGSAPYTKI GTTAGNTMDY GVPASTSGWF KVSASNSAGE
SEPSAALHFQ P
//
