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Database: UniProt
Entry: B0KD85_THEP3
LinkDB: B0KD85_THEP3
Original site: B0KD85_THEP3 
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
//
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