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Database: UniProt
Entry: J9S216_9ACTN
LinkDB: J9S216_9ACTN
Original site: J9S216_9ACTN 
ID   J9S216_9ACTN            Unreviewed;       613 AA.
AC   J9S216;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Penicillin-binding protein transpeptidase {ECO:0000313|EMBL:AFR48686.1};
GN   ORFNames=KTR9_2049 {ECO:0000313|EMBL:AFR48686.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR48686.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR48686.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR48686.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(2012).
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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DR   EMBL; CP002907; AFR48686.1; -; Genomic_DNA.
DR   RefSeq; WP_014926484.1; NC_018581.1.
DR   AlphaFoldDB; J9S216; -.
DR   STRING; 337191.KTR9_2049; -.
DR   KEGG; gor:KTR9_2049; -.
DR   PATRIC; fig|337191.3.peg.2342; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_025328_0_0_11; -.
DR   Proteomes; UP000003281; Chromosome.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR007887; MecA_N.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 1.
DR   Pfam; PF05223; MecA_N; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..613
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039372141"
FT   DOMAIN          35..142
FT                   /note="NTF2-like N-terminal transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF05223"
FT   DOMAIN          331..587
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   613 AA;  64192 MW;  70F3D942CC3A70A4 CRC64;
     MWRMRTRWTP AVIVALCAAV TVATVGCSAS EDDGPRRAAE RFLQAYADRE VASAAALTDA
     PGVAESAMES AWAGLGAEAL ESQAGRVRVT GDTAEVDVDY QWALPRGRDW TYDATLRMGR
     SDDGWAVRWA STNIHPKLGA DQRLSLQIVE APRATVNEAD GSEVMVNGSV VGVNFDPVDA
     AEQGASIAES VTAAVAVLRR FSPSLDEQTI TEQVTANRQQ YPLARLSHEQ FDRLRDQLAI
     PGVVTNEQAE LVPEDPRFAP ALLTEVKKVV DSEVSGRAGW RVVTVNPNGL DADVLADHDP
     DPAPAVSLSL SRTVQNAAQR AVNATNRFQI ALVAVQPSTG RILAVAQNPA ADRQGPIATT
     GLYPPGSTFK MVTAAAAISR RMATPDTPVG CPGAIQIGPR LIPNYDGFSL GTVSMLRAFA
     QSCNTTFAKL ASQMGPSDLA HAAAAMGIGQ QYEIAGLDAV SGSVPIENEL VARSEDGFGQ
     GKVLVSPLGL ALVAATVANG TKAPVPQLIL DKPTKVEGPT PTMAPEVYDQ LRPMMRAVIT
     SGTASVIDGQ GAVFGKTGEA EFAGGSHAWF AGYRGDIAFA TLVVGGGDSN NAVAVTRDFF
     GGLGPGYAVR PLP
//
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