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Database: UniProt
Entry: K4INA8_BIFAP
LinkDB: K4INA8_BIFAP
Original site: K4INA8_BIFAP 
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
//
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