ID D5X7Z2_THEPJ Unreviewed; 838 AA.
AC D5X7Z2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
DE Flags: Precursor;
GN OrderedLocusNames=TherJR_1863 {ECO:0000313|EMBL:ADG82712.1};
OS Thermincola potens (strain JR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Thermincolaceae;
OC Thermincola.
OX NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG82712.1, ECO:0000313|Proteomes:UP000002377};
RN [1] {ECO:0000313|EMBL:ADG82712.1, ECO:0000313|Proteomes:UP000002377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JR {ECO:0000313|EMBL:ADG82712.1,
RC ECO:0000313|Proteomes:UP000002377};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT "Complete sequence of Thermincola sp. JR.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000256|ARBA:ARBA00002624}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
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DR EMBL; CP002028; ADG82712.1; -; Genomic_DNA.
DR RefSeq; WP_013120724.1; NC_014152.1.
DR AlphaFoldDB; D5X7Z2; -.
DR STRING; 635013.TherJR_1863; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; tjr:TherJR_1863; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_2_9; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002377; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; 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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002377};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 75..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 347..617
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 786..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 92582 MW; 093E135C4966B474 CRC64;
MTLEPSKPVN KKPKPKKRRK LNLFRLFLFL VIVAGLLLVG AVSGIVLASI KDVPAFDPKA
LEPNLPTYIY DINKNPVTKI YVENREPIKI QDVPNLVKNA FLAIEDVRFY DHKGIDLRRI
IGAAIVDIKE GRAAQGASTI TQQLVKKAFL NPDKNIKRKI QEVVLAIKLE REYTKDQILE
MYLNRIYFGH GAYGLQSAAQ IYFNKDVKEL TLDEAAVLAG LPQAPSAYDP YRNPEAALKR
RNVVLDMMAK YDFISQAQAE EAKNKAITLK NSGEDGKKEE YPHPYFVDYV TDVLLEKYGE
NKVFKGGLKV YTTMDPKIQT IAEQAMANPN NFPRSKTDKN GLKQPEGALV ILDPHTGYIK
ALVGGREHSQ KLQFNRATDA KRQPGSAFKP IIAYAPAIEK GAGAGTVVVD EPVTFGKYKP
ENSDGKYRGP ITLREAVTHS VNVVAVKVLK DTGITNAVKF AKKLGITSLT QEDENLALAL
GGLHYGVTPL ELAGAYGAFA NKGIYIQPTA IIKVEDRYGK VIDEFKPRKR IAMKDTTAYI
ITDMLKSVVQ RGTGTRASLG KRPVAGKTGT TNQGKDIWFA GYTPELVGVV WMGHDDPKPM
PRTYGGTYPA KLWKEVMSKA LKDREIKDFD KPAGLVKVAI CTLSGKRAGK NCPQSEIRSD
WFVRGTAPSK ICNDHTYVSV EVCADSGLLA TEYCPNKITR SFLKRDKEHT YSSSDIYVPT
QTCNIHGPNN RVISICTDPS HGGTRYLANI PGPGETGGCP PEYVVKETLG AGETAPLEHC
PIPEHQVYPK SPDNPEIIQP EINQKPEKPA KPGKVNLPAQ PEITTQNYQE KDKRKGLP
//
