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
//