ID A0A1I3H0C6_9BACL Unreviewed; 1045 AA.
AC A0A1I3H0C6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN02799624_00156 {ECO:0000313|EMBL:SFI29111.1};
OS Paenibacillus sp. UNC496MF.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1502753 {ECO:0000313|EMBL:SFI29111.1, ECO:0000313|Proteomes:UP000198714};
RN [1] {ECO:0000313|EMBL:SFI29111.1, ECO:0000313|Proteomes:UP000198714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNC496MF {ECO:0000313|EMBL:SFI29111.1,
RC ECO:0000313|Proteomes:UP000198714};
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; FORE01000004; SFI29111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3H0C6; -.
DR STRING; 1502753.SAMN02799624_00156; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000198714; 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; 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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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; 2.
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:UP000198714};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 823..919
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 958..1045
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 906..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 114286 MW; D877FCA6BC7289E7 CRC64;
MDQDRQQKPK SYSKWRTFGI VTFVTIKWLF IFGLLIGLLA GAAVAGYVAS FVKDEPVRSR
AEIEAKIDEN AVTGFVYFND GQTPVGQLRT EEDRRLVKRN EIPPQVVNAV LATEDNNFYK
HIGVDFNGLA RAVKQKLLNE DTQTGGSTLT QQLARQVFLT LDKTDSRKAK EIFLALRLER
FMTKDEILTA YLNKVQFGTS NSGYNLYGIK AAAKGIFNIT DLNKLNIAQS AYLAGLPQRP
SAYTAFTSKG KFNPDGFKLA VDRQHIVLRR MLETGRISQE QYDEAMSFDL EKSLAKPTEK
AYSTFPFLML ESERQASVQL MLAENPNLKP EDVNKKENAQ LLEEAHEHLL RGGYHIYTTI
DKKVYNAMHK IGSDPNNFGG DSKEKGIEQT GAVMLDHKTG AILGMLEGRD FYTEQLNHAT
QMTRQPGSTM KPIAAYLPAI EKGIIQPASV IDDSPIVMKD GQKGFHIPMN VTNKFYGLVT
ARDALNRSLN IPALKIFNNL VTIPEAWKFA RKLGITTIQP QDDYAQTGVI GGLSIGVSVE
ELTNAYGAIA DKGEFNDAYM ISKITDANGK VVYQHADKPL RVFSEQTAFL MTDMMRTVIS
DPSGSGHKIT SYFKNYGKIP VVGKTGSTQS YGDVWFMGFT PDITLGVWVG YEKQKYTLSK
PERERARIIW SDIMNEVTTT RPELFPTKEF TMPSGIVKAT VSRLSGKLPT DLTRSEGKLV
TDWFNTKFVP KEPDDALVRM AVISYNGINY IPKPTTPSDM VKEQLVVKRQ KPLDELMKEI
EAAQAKLPAD SRRPMSAYVP ADAGRDAPSM VDPRVDDGRA PSPPSNVGIE TVSGGGAYRI
TFKASPERDV VGYRLYRSVN GGAFANMNNP VLTGQDSRFV NYINAPGGYA YYVTAVDVAG
KESAPSAVVN SGGGIAPPPD QGSASPTDTG SVGDIIGLPT GNGNGSGGQP GSNPGLASPS
APIHIAIEST AIGIKLTWAD NATSEQVTGY NVYYSTDGSG TFKKIGSTNE TRFEYVSPLT
SGYFRVTAVN DAGESPPSAP AAIQP
//
