ID B2TKL8_CLOBB Unreviewed; 678 AA.
AC B2TKL8; U4P5E1;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Penicillin-binding protein 3 {ECO:0000313|EMBL:ACD22580.1};
GN OrderedLocusNames=CLL_A0618 {ECO:0000313|EMBL:ACD22580.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD22580.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP001056; ACD22580.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TKL8; -.
DR KEGG; cbk:CLL_A0618; -.
DR PATRIC; fig|935198.13.peg.565; -.
DR HOGENOM; CLU_009289_5_2_9; -.
DR Proteomes; UP000001195; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..151
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 160..326
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 359..675
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 678 AA; 75978 MW; 54DDC36BF774C36E CRC64;
MEKKIKRLFI FSLIIIGILV VAAFIFASMK ANSINVKQSE KLLQEYFELL NEKKYDLMYD
KLSDESKNEI SKESFIERNK NIYEGIGAKN ITIDSIKVKV DGSDILATFQ CNMNTIAGNL
NFNNTMEIYR IRDEIKVNWS SNLIFPELNN DYKVKVQITD SRRGDILDRN NIKLATDDDV
AEIGIVIEEL GENQKESINE ISKELEVPSE YIEKQLSQSY VKPNMFVPIK VVSYNNEMVN
KVLKFPGIAI KDKPSRVYPL EEKAAHLIGY IQNVTAEDLE KNSDKSYSAS SVIGKSGLEA
IYEDRLRGID GIKINIVDKN SNEIKVIYNR EVKHGEDIKL TIDSALQQTA YDALEDNNGA
TVSINPNTGE VLALVSTPAY NPNDFVLGLS TEKWNDLNTN ESKPLYNRFQ SNITPGSAFK
PITAAIGIEE NVLDPNEDKG IVGLKWQKDD SWGGYKVTRV HAYSLPANLE NALIFSDNIY
FARVALDIGA ENFEKKLKEF GIGEKIPFEY GVSVSQFSSE DGINNEILLA DSGYGQGNIL
MNPLQLSMMY TMFTNEGNIL KPYLEYKENS EKSVWKNNVI SRQTAEIILN DLHSVVSKPN
GTAHALFEQG INIAAKTGTA EIKLAQDDES GTEIGWVVAT TTNKENNILV TTFVEDVKDK
GGSGYVIPIV KKIIQEMK
//
