ID Q2LXN6_SYNAS Unreviewed; 674 AA.
AC Q2LXN6;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Multimodular transpeptidase-transglycosylase {ECO:0000313|EMBL:ABC78847.1};
GN ORFNames=SYN_00304 {ECO:0000313|EMBL:ABC78847.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC78847.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC78847.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC78847.1,
RC ECO:0000313|Proteomes:UP000001933};
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
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 -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CP000252; ABC78847.1; -; Genomic_DNA.
DR RefSeq; WP_011418863.1; NC_007759.1.
DR AlphaFoldDB; Q2LXN6; -.
DR STRING; 56780.SYN_00304; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; sat:SYN_00304; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_4_7; -.
DR InParanoid; Q2LXN6; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001933; 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF27; 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 3: Inferred from homology;
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:UP000001933};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..242
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 337..573
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 636..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 75082 MW; 8F24663F213A380F CRC64;
MVKTSQHPVT RNRCSAGSIL IVLVFFLLLA LLVGSSILYY VVLRDLPSIA ALKEYRPSIT
TRVYADNNEL IDEFYMENRK LVRFEEIPSL VIKAFLAAED ARFFEHRGFD VQSISRAFFR
NLRAGRIVQG GSTITQQVAK ALYLSSEKSY SRKIKEAVLA YKIDRSLSKK EILNLYLNHI
YLGHGAYGIE AASQVYFGKR TRDLKLSEAS LLAGLPKAPS SYDPYTSYQR ARQRQTYVLS
RMVEDGHITE EEKNHVLQTP LPLRSIRPRD RVAAYFIENI RRYIQGKYGS DALYKEGLEV
YTTLDIRTQQ AARDAVERGL KELESRQGYS RDMVQGALLC MDARTGAIRA MVGGRDFSKS
EFNRATQSRR QPGSAFKPII YAAAFDRGMT PATEIVDAPL AFEDGMGHAW TPQNYDEEFL
GPISLRTALV QSRNVVTIKL LQEIGVDYAI AYAANMGISS RLARDLSLAL GSSAVTLQEL
VRSYAVLANG GKIVEPFMIK KIVDRTGYVF EEHTIKVEQA IDPRIAFLTT SILQDAVESG
TGQRVKSIGR PVAGKTGTTN DVHDAWFVGF TPSLVTGVWV GFDQQRPLGN QEVGGLAAAP
IWLYCMERAL ANKPVESFPV PDGIVFVRRN EGALPEPFID GTAPPDAIPA DAEGSTSTEE
EGEEDPGWKF RFPF
//
