ID B0KD85_THEP3 Unreviewed; 829 AA.
AC B0KD85;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 24-JAN-2024, entry version 92.
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=Teth39_1978 {ECO:0000313|EMBL:ABY95604.1};
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY95604.1, ECO:0000313|Proteomes:UP000002156};
RN [1] {ECO:0000313|Proteomes:UP000002156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E
RC {ECO:0000313|Proteomes:UP000002156};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) 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; CP000924; ABY95604.1; -; Genomic_DNA.
DR RefSeq; WP_003867048.1; NC_010321.1.
DR AlphaFoldDB; B0KD85; -.
DR STRING; 340099.Teth39_1978; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; tpd:Teth39_1978; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_2_9; -.
DR OMA; QQNTGGD; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002156; 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; 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 Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:ABY95604.1};
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:UP000002156};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000313|EMBL:ABY95604.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..260
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 367..621
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 762..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 90975 MW; 3C6BF6BB61DB977A CRC64;
MDNNANLKRS ERRKQKDKTK KKSVAKNIIK FVIYTFIILI FAAAGVIGAK VWTIIKDTPE
ISEEALTKQA QSSIVYADNG EEVATLFGAS NRIWVPLDQI PKDLQNAFVA IEDQRFYQNN
LGIDPKRIIG ALIANIKAGG KPVEGASTIT QQLVKNTMLS SEKTLSRKIK EAILAWRLEQ
KYSKEQILEA YLNTIYLGGP NVNAYGVEAA ARAYFNKHVN ELDLAESALI AGITKNPSLY
SPAANKEAAI ERQRLVLKEM LKQGYITQEQ YDEAINEKLE FDIHYSVVSD KHKYFIDQVK
EDVANALSQK LNISYEEAMN KIFNGGLRIY TTMDVNIQNI MEEAFKNSKL FPADLKDKEG
NIRIVQGAMV VMDWRTGEVK GIVGRRETDE TQGKVRVFNY ATTGGRPPGS SIKPITVYGP
ALEKGYTAAT VVDDVPVYYK QWNWEPHNYS RNTYKGLMTF REALKVSQNI PAVRIVVEMI
GLNTAAEYGK KFGLDITERI EKSPAALSLG AGGEVTPLQM AAAYGAIANG GVYTSPITFT
KVTDSEGNVI LENKPSQHIV LSPQNAYILT NMMQEVVKPG GTGTNARLPN MPVAGKTGTN
ENYYDAWFAG FTPYYSASVW MGTGENIAMI YGGKGVTGGS YPAIFWKTVM MQIHKNLPYK
DFVRPPGIIS VTVCRDSGEL PTDLCHLDPR GDRTYTEIFA QGTQPTTYCT VHVTAKINSQ
NGKLATDLTP PDLVKDAVFI DPPGRTPAQN AVALDGKYVV PKEYDDTVPP PQNSDNGDAP
GDNTQPPPAN NGGTEQPPGG ETTNPPPNNG NSQTSPPSNN PPSTTNPIP
//