ID S2ZQ54_BIFBR Unreviewed; 788 AA.
AC S2ZQ54;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-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=HMPREF1482_00259 {ECO:0000313|EMBL:EPD76485.1};
OS Bifidobacterium breve HPH0326.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1203540 {ECO:0000313|EMBL:EPD76485.1, ECO:0000313|Proteomes:UP000014395};
RN [1] {ECO:0000313|EMBL:EPD76485.1, ECO:0000313|Proteomes:UP000014395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPH0326 {ECO:0000313|EMBL:EPD76485.1,
RC ECO:0000313|Proteomes:UP000014395};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dover J., Dai D.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bifidobacterium breve HPH0326.";
RL Submitted (MAY-2013) 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:EPD76485.1}.
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DR EMBL; ATCB01000001; EPD76485.1; -; Genomic_DNA.
DR RefSeq; WP_016462106.1; NZ_KE150453.1.
DR AlphaFoldDB; S2ZQ54; -.
DR PATRIC; fig|1203540.3.peg.253; -.
DR HOGENOM; CLU_006354_6_2_11; -.
DR Proteomes; UP000014395; 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 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 69..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 120..292
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 384..625
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..788
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 23..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 84794 MW; A3115539F74CC754 CRC64;
MASYKRRAHS SDRGPALRKP RATQSKTAGT TKTSSTRGPR GKNNTSRKPA NTHRASSHKR
NGGHRVLKWV LGIFFGLIGL GLAIGIGVFA YLYATTEVPQ PEKFALAEKT TVYYADGTTP
IGSYAEQNRE IISCEGLPDY VGNAIVASEN RTFYTDKGLD LKGIARAFIN NVTKGTRQGG
STITQQYAER YYMGETTSYV GKAREAIIAI KIAQTESKDE VLCNYMNTIY LGRNSYGIQA
AAKSYFNKDA KDLTLSEAAM IAGIIPSPST WDPADNPDMA KARFKRVLNI MQEDGYITAK
DHKAAEFPQT ADVTQQNEYA GPNGYLLDMV RRELVASKTF TKEDLDTGGY KIVTTIDKAK
QDAMQSVGDT RADGMPESIQ VGGIAVEQKT GAVVSVYAGS DYLTQQLNNA DQAMFEPGST
MKPFALLGAA QSGVNFDTMF NGNSHQHFSG ITAEVNNALN INWGNINLYQ ATANSVNTVF
MNVNEHLTPQ RTAKIAHEAG IEGEIDTSSM YNVLGINALT VWDLAQGHST IANNGVKNTL
HMVNKVLSSD NKDLYNAPNE NKQVFDANDC ALVQKAMQGT TTYGTAAGVS SALGGRQVAG
KSGTANDELA ASFVGYTPSL LNVWAIWNPD ADGNPQVVPA FGGYGVTSTG YPAHLFEEYM
TQALQGTAVE QFTTPKDSGK IGGSDGTWGL GGGQSSSSST TDDEEAKKQA EEEAKRKAEE
EAKKQADAEA QQKQEFAQQC LANPSYSTEC PNYPGTSSGG DGDTDVDPQP KPDPQPKPDP
QQPQSQQQ
//
