ID A0A1B9AI68_9BACI Unreviewed; 908 AA.
AC A0A1B9AI68;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A8L44_11935 {ECO:0000313|EMBL:OCA83533.1};
OS Bacillus sp. FJAT-27986.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA83533.1, ECO:0000313|Proteomes:UP000092673};
RN [1] {ECO:0000313|EMBL:OCA83533.1, ECO:0000313|Proteomes:UP000092673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA83533.1,
RC ECO:0000313|Proteomes:UP000092673};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J.,
RA Liu B., Liu G.;
RT "Bacillus sp. FJAT-27986.";
RL Submitted (MAY-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 -!- 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:OCA83533.1}.
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DR EMBL; MAYV01000016; OCA83533.1; -; Genomic_DNA.
DR RefSeq; WP_066107360.1; NZ_MAYV01000016.1.
DR AlphaFoldDB; A0A1B9AI68; -.
DR STRING; 1743146.A8L44_11935; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000092673; Unassembled WGS sequence.
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; 1.
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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000092673}.
FT DOMAIN 697..787
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..800
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 99722 MW; 1D3EC996D93BC568 CRC64;
MSDQYKTRTE KRKYANSKRN KKQKKQSKSL LKRTLIVLAA LFIIAGISVG GVFAYWAVTA
PEIDDSALID PISSKIYDKN GDIYTEVGSE TRDYVDYKDV PKLMENAILA TEDVRFYKHH
GIDIIRVGGA LIGNITGGFG SQGGSTITQQ VVKNSFLKSE KTIKRKVQEM YLAFQLEQKY
SKEQIFEMYV NKVYMSSGVH GFSTASKLYF GKELNELTLS EAATLAGMPQ SPNNYNPFTY
PEKAEKRRNI VLKLMEKAGF ITAEEHEKAQ AESVEDSLVP EEKREKTTNT KYNAIVDQVI
DEVEEIGDYN IYTDGLQVYT SIDPDAQELM EEILNSDKYI DYPNDKFQAG TVFMDTKTGE
INAMGGGRNQ EVARGFNYAT DLKTRQPGST IKPILDYGPA IEYLKWSTAH IIKDEPYKYS
SGQSIGSATG TYKGNVTIRE ALYKSLNVPA VKTLQEVGED QAGKFAKKLG VDFGEIYEAS
AIGGVDKAAS PLQMAGAYAA FGNEGIYNKP HVVKKVVLRD NDTVIETAPE PQVAMKDYTA
FMITNILQDV VTKGTGTAAN IPGLHIAAKT GTTNYSAEDR AKYNISKSSS PDAWFIGYTT
NYTMSVWTGY DQQLKNPMSK QETKIAAKIF KTMMGKMSEN VTTDNFKQPS SVVKVALEKG
TNAKASEYTP SDQIVYEYFV KGHEPTKTSE KYTKPNAPSG LNAAFDEASN RINVSWKYDS
SNDAEFNVQV AVDGGDRQTL TTTKETSFSL DAPEAGKKYT FYVTATVDGQ ESDSASTSVS
IPEAAPEEEE QPEEPTEDNT EDPNQPNPDN GTGNEEDPNE GNNPEEGTNP GEGTNPGEGT
NPGEGTNPGE GTNPGEGTNP GEGQPEPQDE DGQEQPAARS NSTSQPDETS YLIPPAIQEM
PRHIRKIA
//
