ID A0A140DT19_9FIRM Unreviewed; 849 AA.
AC A0A140DT19;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=AALO17_06620 {ECO:0000313|EMBL:AMK53796.1};
OS Faecalibaculum rodentium.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalibaculum.
OX NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK53796.1, ECO:0000313|Proteomes:UP000069771};
RN [1] {ECO:0000313|EMBL:AMK53796.1, ECO:0000313|Proteomes:UP000069771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alo17 {ECO:0000313|EMBL:AMK53796.1,
RC ECO:0000313|Proteomes:UP000069771};
RX PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA Lim S., Chang D.H., Ahn S., Kim B.C.;
RT "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT C57BL/6J laboratory mouse feces.";
RL Gut Pathog. 8:3-3(2016).
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; CP011391; AMK53796.1; -; Genomic_DNA.
DR RefSeq; WP_067555416.1; NZ_CP011391.1.
DR AlphaFoldDB; A0A140DT19; -.
DR STRING; 1702221.AALO17_06620; -.
DR GeneID; 78477482; -.
DR KEGG; fro:AALO17_06620; -.
DR PATRIC; fig|1702221.3.peg.640; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000069771; Chromosome.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000069771};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..267
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 373..630
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 803..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 94061 MW; 75C79E366CA32DB5 CRC64;
MPEKETSGSQ RPAAAKSARR RKLDIWNKIA VAILTCFLVG CISVFFILVN VINDPDGMRF
SQEGLSTLSN SRMFDTDGNL IYEFGNEIRE DVTYDQIPQS VVDAFLSIED SRFYDHHGFD
LPRFLAAALS NLRSGTLGQG GSTLTMQMID NAFTKIQEDK IKAEEGSVSK LESIKLKIQE
IYLALIAEQS ISKEDIFDYY VNRIWFGSSY NTRGIQKAAE YYFNKDVSQL NLGEAAFLAG
AVNSPASYNP INNKYAAAED ATDYLQSATN RRNVTLKLML DHGYITEEEY ELAKNSRLEF
ALLETDMSTN DPNMPFIQQA IEEVQTLAGQ DPFVIPMDIY TSLNQGAQKQ CDDILRGRVD
SVQYPNDAFD VGFSIIDNAT GEILCVGPGR RYIQGQTDRD NSLDRKQPGS SMKPLLAYAP
TFDLLGWSTV HTVNDKADDY FTTGQNLQNS DRRYQGLMSL QDALGVSKNT TAAAAMNDLI
AATGLEYWQD YCRKLGYDQD VWEQFVAQYA IGGSNMWASP IQQASAYTIF ANHGNRVNAH
RVRRIVRRAD KEEIAGNTTT EELISDQAAF MMSSLLEKVV TGGYQNFNEI LKSSYTVYGK
SGTSDWGVYG QQYGIPNGAI RDEWSVGYTN RYTIATWSGY TEEFQQQGYY INDQQLYMAT
AFHISHYMLD YMEQFGGYSP IARPDGVSDY KSGYIKTEFV DKGDETAPTY NTYQPSESEI
RSACQASGGT YDEEAGICIT KQEDDSAATA CTGSGGTWDG TACSCPDGYE LNGTACEAID
QSDPSAECGA QGGTWNGTYC EFPTQPEVPD SGGDDSVTGS ENGETGGLIP PTGLIVPRFF
GLFNLFNWL
//
