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Database: UniProt
Entry: A0A0F4M0G8_9LACO
LinkDB: A0A0F4M0G8_9LACO
Original site: A0A0F4M0G8_9LACO 
ID   A0A0F4M0G8_9LACO        Unreviewed;       885 AA.
AC   A0A0F4M0G8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=JG30_00200 {ECO:0000313|EMBL:KJY63341.1};
OS   Bombilactobacillus mellifer.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Bombilactobacillus.
OX   NCBI_TaxID=1218492 {ECO:0000313|EMBL:KJY63341.1, ECO:0000313|Proteomes:UP000033558};
RN   [1] {ECO:0000313|EMBL:KJY63341.1, ECO:0000313|Proteomes:UP000033558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin4 {ECO:0000313|EMBL:KJY63341.1,
RC   ECO:0000313|Proteomes:UP000033558};
RA   Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA   Vasquez A.;
RT   "Comparative genomics of the lactic acid bacteria isolated from the honey
RT   bee gut.";
RL   Submitted (JAN-2015) 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:KJY63341.1}.
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DR   EMBL; JXJQ01000001; KJY63341.1; -; Genomic_DNA.
DR   RefSeq; WP_052725135.1; NZ_KQ034028.1.
DR   AlphaFoldDB; A0A0F4M0G8; -.
DR   STRING; 1218492.JG30_00200; -.
DR   PATRIC; fig|1218492.5.peg.131; -.
DR   HOGENOM; CLU_006354_2_3_9; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000033558; Unassembled WGS sequence.
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   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:SF33; PENICILLIN-INSENSITIVE TRANSGLYCOSYLASE; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000033558};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          79..252
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   COILED          772..866
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   885 AA;  101460 MW;  927F760528014435 CRC64;
     MTNNFRHWWH NFLQHPLRKL IKYCGWLCLL VGLIWGGWKL HQGVNALKKD ITDGYLISDT
     VSKQTFYPKQ PTVIKDNQGK VMKKLTHSQA NYISFTKIKP IVRQGMVASE DRRFYQHHGV
     DLYGVLRAMV QLVLRRQIQG GSTLTQQLVK NVILKDQSQN FHRKIKEMVV AQSLEKKFTK
     QQILEFYLND VYLGHGCYGI GSAARYYFSK PQSRLNYSEA ALLIGIPNNQ ILYDPVTHPQ
     TARNRRNTIL YTWKQQKLIT AAQFTKYSQQ PLNLKIHNFQ YDNDISHDYA LNYAVSNAVK
     QLMAVHGFEM QYLFADDQAK TNYKNQYTQA YEKYYGELLK GGFIIQTTIN RDLQQKVVAA
     VQAQYTKYQT RDADGKLEPQ VASTIVDNRS GDVLALVGGR TTDGDQLNRA IDAFRQPGST
     AKPIIAYAPA FERGYFPQSK VIDGPIANVH NWYSGYRGAV TLRTALADSI NTVAFKLAAN
     DKDYSFYNDL GKMEFSGLYP ADKNPITAVG GFTKGVTTTE MAAAYSSFAR SGRFVSPSNL
     RSIYDTVNNR WLYQNTHLKT EVYSKNASYM MINAMQSVVN SGSGKGARLD NYPYVAGKTG
     TTDNNNDSYF VGMTPSFTIA NWTGYDHQTS LTAEELQLPI KTFKAEGQLL VDYLKEAKTD
     FPMPNTIRRE GDYLFVRNNA NQKTVAQIIE QNYVAFNSAQ INANQMRLNN LDYRLIYHLS
     KKQERQREKQ VELALQRYTS LPFTQLSQYD DKVAELQKIR YKNENVKRMA AKNEFNKTIM
     QLQSKLNLTQ AKLQAQKENR RLAKFEQQKQ QIQAQRDAKR RSLVDRLMRQ YSTQLQRVQT
     AYDNNAADKE LQLQKLENLI NQIRSYGGTV DDPVITVHHN KNNGN
//
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