ID F7QV98_9LACO Unreviewed; 772 AA.
AC F7QV98;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=LSGJ_01036 {ECO:0000313|EMBL:EGM50490.1};
OS Ligilactobacillus salivarius GJ-24.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1041521 {ECO:0000313|EMBL:EGM50490.1, ECO:0000313|Proteomes:UP000003074};
RN [1] {ECO:0000313|EMBL:EGM50490.1, ECO:0000313|Proteomes:UP000003074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GJ-24 {ECO:0000313|EMBL:EGM50490.1,
RC ECO:0000313|Proteomes:UP000003074};
RX PubMed=21742893; DOI=10.1128/JB.05616-11;
RA Cho Y.J., Choi J.K., Kim J.H., Lim Y.S., Ham J.S., Kang D.K., Chun J.,
RA Paik H.D., Kim G.B.;
RT "Genome Sequence of Lactobacillus salivarius GJ-24, a Probiotic Strain
RT Isolated from Healthy Adult Intestine.";
RL J. Bacteriol. 193:5021-5022(2011).
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:EGM50490.1}.
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DR EMBL; AFOI01000004; EGM50490.1; -; Genomic_DNA.
DR RefSeq; WP_003706335.1; NZ_AFOI01000004.1.
DR AlphaFoldDB; F7QV98; -.
DR PATRIC; fig|1041521.3.peg.1038; -.
DR Proteomes; UP000003074; 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; 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 37..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..262
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 359..641
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 83536 MW; 006DC5A760D96547 CRC64;
MDSNENSRLS RVAKRREEES RNNPRKPNKN SGLVKKIILG ALTALLALFV IGATVFFVYA
KNAPELSENK LTSAGNSVIY DANGDKITSL GNENRTYIKT EDIPQQLKDA VVSIEDRRFY
KHHGVDPVRI VSAALSNVTG SSAGLQGGST LDQQLIKLSF FSTKKSDQTL KRKSQEAWLA
MQLDKEYSKE QILTFYINKV FMGYGTYGME TAAKYYYGKS LKNLDLAQTA MIAGIPNAPS
TYNPYSSPKL ATQRRNDVLD AMVANKKISQ AQANEAKQED VTDGLVQTHE QESTTSQKAK
ISDSYLKEVI AEAKEKGYDP YSGNLKIYTN LDMDAQKKLY NIVNTDYYVD FPNDTMQVAT
TVVDPNNGKV IAQIGGRKTG DVTYGLNRAV QTDRSSGSTA KPVMDYAPAI EYLDWATYHA
LKDTKFYYPG TSTQLYNIDN RYKGTITMRQ ALIESRNVPA IRALQAVGMT KAKSFLSNLG
YDTKGLSLQN GIGLPASTLQ NAAAYAAFAN GGTYYEPTYI DKIETADGQV NDYSSSGKRV
MQSSTAYMIT DMLKQVITSS NGSGTAANIS GLYQAGKTGT TDYPSDVSGQ FPSDAAMDSW
FDGYTKHYSI SVWVGYDHQY EPGNYVPNNS KLAQQIYKVL MTYLSQGVSN TDWTKPSNVY
SRTINGQREL YLAGSAAPTI TGKGSSSGIN ESSSSSSSSS SDKESSGSTS SSDEKSSGSD
SNSNASESST STASSTSANS SATTTTGGNN NTQSNNTPAT PAGNNGGNQA GH
//
