ID A0A248TM43_9BACI Unreviewed; 878 AA.
AC A0A248TM43;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=CKF48_19115 {ECO:0000313|EMBL:ASV69232.1};
OS Cytobacillus kochii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX NCBI_TaxID=859143 {ECO:0000313|EMBL:ASV69232.1, ECO:0000313|Proteomes:UP000215137};
RN [1] {ECO:0000313|EMBL:ASV69232.1, ECO:0000313|Proteomes:UP000215137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BDGP4 {ECO:0000313|EMBL:ASV69232.1,
RC ECO:0000313|Proteomes:UP000215137};
RA Wan K.H., Yu C., Park S., Hammonds A.S., Booth B.W., Celniker S.E.;
RT "Complete Genome Sequence of Bacillus kochii Oregon-R-modENCODE STRAIN
RT BDGP4, isolated from Drosophila melanogaster gut.";
RL Submitted (AUG-2017) 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};
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DR EMBL; CP022983; ASV69232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248TM43; -.
DR KEGG; bko:CKF48_19115; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000215137; Chromosome.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000215137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 698..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 770..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..878
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 96911 MW; E9B42E6F8B5975C9 CRC64;
MSEQYKSREE RRKQQQQSPK PKKKKSGKTL FKKIFLTLIA LGIVGMIAGA ATFAFMVKDA
PELDPALLKD PIPSVLLDIN GEKITEVGAG NLDYVEYEDI PDLVENAFLA TEDVRFYEHN
GMDLIRLGGA VIANVTKGFG SEGASTITQQ VVKNSFLNNE KTISRKAQEA WLSFQLERKY
TKQEIFEMYV NKIYMSENSH GVLTASRLYF GKDLDELELH EAALLAGMPQ SPNNYNPFTH
PENAEKRRNI VLSLMNQHGF ISEEQKTEAQ SIPITEGLVP EGEREIEDDT PYDSFVDVVI
DEVTEKYPDL DIFSDGLTIH TTADKDIQKY VSNILNSEDV IQYPDEEFQA GITLLDSSNG
EVRAIGGGRN QEVKRGFNFA TDQKRQAGST FKPIAGYAPA IEFNQWGTYH TLVDEPYKYS
EGTEVNNWDN SFKGTMTMRQ ALAESRNIPA VKAIQEVGTE QSMEFANRLG FNFKDEYYES
SVLGTKAVSP MEMAGAYSAF ANEGFYTDPH TVKAIEMRDG TKIDTTPESE AVMNDYTAFM
ITDMLKTAIS SGTGTTANIQ GLPVAGKTGT TNYTAEEKQK YDIPNGATPD AWFAGYTTNY
TAAIWTGYES RKTYLPSNGY DQKIAQMLFK NIMQYASEGK ETADFKMPNS VEKVAIEKGS
NPAKLASEYT PSDQIITEYA VKGNAPKTVS EKFDKLEAPN GFNAKYNKEA NTIELVWKHK
DKDNTQFVVT GAINDGGAQE LTTTSETSLT IENPEPDSTY TFTVKAVQDG KESDAAQTSV
NIPSNEEEPE EVEPPEEETP GDGQQPPGDE EGGNDNENGN GDGNNSENGD GNGNNNGEGN
DNNNGNENGN GNGNEDNSEE ENQSPEEEPS PPDENPEE
//
