ID K4INA8_BIFAP Unreviewed; 748 AA.
AC K4INA8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=BAST_1538 {ECO:0000313|EMBL:AFU72107.1};
OS Bifidobacterium asteroides (strain PRL2011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU72107.1, ECO:0000313|Proteomes:UP000007006};
RN [1] {ECO:0000313|EMBL:AFU72107.1, ECO:0000313|Proteomes:UP000007006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRL2011 {ECO:0000313|EMBL:AFU72107.1,
RC ECO:0000313|Proteomes:UP000007006};
RX PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA Ventura M.;
RT "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT colonization of the insect gut.";
RL PLoS ONE 7:E44229-E44229(2012).
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; CP003325; AFU72107.1; -; Genomic_DNA.
DR RefSeq; WP_015022543.1; NC_018720.1.
DR AlphaFoldDB; K4INA8; -.
DR STRING; 1147128.BAST_1538; -.
DR GeneID; 41010747; -.
DR KEGG; bast:BAST_1538; -.
DR PATRIC; fig|1147128.3.peg.1563; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_6_2_11; -.
DR OMA; LAQMAMI; -.
DR Proteomes; UP000007006; Chromosome.
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 Glycosyltransferase {ECO:0000313|EMBL:AFU72107.1};
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 Transferase {ECO:0000313|EMBL:AFU72107.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..278
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 377..614
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 80635 MW; 16A3C50326DEDA86 CRC64;
MANQTRSVSS TSPTRRIQSG ASGGRNRADR LTSRHADRNP RGGGPRRRRP HKKSHRVLKW
TLALLGLVLV AGAAAFAYLY LTTEIIPPEK QALAQKTTVY YADGTTPIGT YADQNREIID
CAVLPKYVGN AVVASENRSF YKDNGIDLKG IGRALLNNVT KGTRQGGSTI TQQYAERYYL
GETTSYKGKL REAILSLKIS RTESKDAVLC NYMNTIYFGR GAYGIQAAAQ NYFGKDAKDL
TMPESAMLAG IIPAPASWDP AINPKQAESR FHRVLGIMEE DHYISRQDRV GAQMPQTIKY
SPQNVYQGPN GYLLRMVRNE LASGKKAPFT ADDLDTGGYR IITTIQKDKQ DLMFQVASPS
TGNKRQPPTL QTGGLSVDPR TGAIISLYAG DDYLTHPLNN VDQATYQVGS TMKAYTLLAA
IQDGVNLNTV FNGNSPRTFS SVGKSVANDG NVSYGYINLY SAFARSVNTV FMDLGEHVTS
QKIAQVAHTA GITGKIDDTT TFDTLGLDAL SVYDVTQGYA TLANGGKRPQ LHLVAQVKDA
KDQELYTAAI QSDQVFNADQ VALLQKAMST TVQYGTATYA RSLGRPIAGK TGTANDQTAI
SFVGFTPSVL TTFAVWNQGQ DGSALRVPAV YQNEFLPVPL FTQYMKSALG NSPVERFPAA
EDHGKIGGPD GSWGTGYRQS YSYTPKRSYN YGYVPQQRSQ QHTAPQQESG AGNGSGSGNG
GGSGNGGGTE DSKSGTTGGN SESESSQQ
//