ID A0A086BNE9_9BIFI Unreviewed; 804 AA.
AC A0A086BNE9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BBOMB_1309 {ECO:0000313|EMBL:KFF30463.1};
OS Bifidobacterium bombi DSM 19703.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF30463.1, ECO:0000313|Proteomes:UP000028730};
RN [1] {ECO:0000313|EMBL:KFF30463.1, ECO:0000313|Proteomes:UP000028730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF30463.1,
RC ECO:0000313|Proteomes:UP000028730};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(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:KFF30463.1}.
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DR EMBL; ATLK01000002; KFF30463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086BNE9; -.
DR STRING; 1341695.BBOMB_1309; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000028730; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; 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: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 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 InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF34; 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; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:KFF30463.1};
KW Glycosyltransferase {ECO:0000313|EMBL:KFF30463.1};
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:UP000028730};
KW Transferase {ECO:0000313|EMBL:KFF30463.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 103..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 154..324
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 424..663
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 86255 MW; D79AFBEB399ECB0F CRC64;
MVSRRQQIPA HIANAQTSRS RRVSSANAIS SRRSRADSAA TSNTPYGGRA NGSTPRNAPT
ARTRERRNTA GKKYVRRGSH TSNATNNRRR RPRNGGGKRR HLVLKWVLGI LAALLAMGVA
AFAYLYATTE VPPPEKMAMA AKTTVYYSDG TTQMGSFAEQ NRDIIECSTL PKYVGESIVA
SENRTFYQDR GIDLKGIVRA LLNNVTGGAR QGASTITQQY AERYYLGQTD TYAGKVHEAI
LALKINKTQS KDQVLCNYMN TIYLGRGAYG IQAASKVYFN KDAKDLTAPE SALLAGIIPA
PSNWDPAINP QMAQKRYTRV IDAMRDADYI SPADADKAKT MPSTQPLRQQ PNWYAGPQGY
LLQMVREELT NSKTFTKNDL DTGGYTIVTT IDKTKQDTMF DVASPTKGGA GIVPAGLQIG
GISANVKNGD IEAVYAGDDY LTKQYNNATQ ATYEPGSTMK PFALLGAVEA GVNLNTTFNG
NSPRTYAGIA TPVQNYGNTS WGYSNLYKAT ADSINTVYMD VQEHLGAKKV AQIAQTAGMD
PKLVTGDNPF TVLGNDGVHV KDVAQAYATI ANQGNKPTLH IVASVKDSSG NEMYRAPVDT
EQVFSANDTG LVAKAMTGTI QYGTAYEARR IGKTIAGKSG SANDDTAGSF VGFTPNIVTV
FATWNPDANG NPQVVPRFGR FTDTAAYPIH LFTEYMSQVL EGTPNQDFPA VKDTGKIGGP
DGKWGTGAPS GTNGGFSQPY RNSANTNPGQ QQQSQGEAAN PDDTNAPKGN ETGSQPGTVP
NETTKPDDSP TQNQSEGSAQ YSGQ
//
