ID Q97D06_CLOAB Unreviewed; 671 AA.
AC Q97D06;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Penicillin-binding protein 2 (Serine-type D-Ala-D-Ala carboxypeptidase) {ECO:0000313|EMBL:AAK81604.1};
GN OrderedLocusNames=CA_C3683 {ECO:0000313|EMBL:AAK81604.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK81604.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK81604.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; AE001437; AAK81604.1; -; Genomic_DNA.
DR PIR; A97352; A97352.
DR RefSeq; NP_350264.1; NC_003030.1.
DR RefSeq; WP_010966944.1; NC_003030.1.
DR AlphaFoldDB; Q97D06; -.
DR STRING; 272562.CA_C3683; -.
DR GeneID; 45000181; -.
DR KEGG; cac:CA_C3683; -.
DR PATRIC; fig|272562.8.peg.3872; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_5_2_9; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AAK81604.1};
KW Hydrolase {ECO:0000313|EMBL:AAK81604.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:AAK81604.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..671
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039113788"
FT DOMAIN 26..143
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 151..319
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 352..665
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 671 AA; 73768 MW; B13976CC57732EDF CRC64;
MKRKYLLLLT LLLTISFTFG CSSSDTPKAS FEKYINAWNK NDYKTMYSIL STDSKKSISQ
KDFVSRYENI YDGIELNKIS VMPEYPSSYK KDSKGNVPIP FKVTMNTVAG KVTFNDTASF
KESNNTWYLN WSSEMIHPDL KKGYKIRIEK TPAKRGEIKG TNGSYLAQNG YIENVGIVPN
KFTGDTEASK KQIADILQVD VNSISKKLSA SYVQPDMFIS IAKLSTDDTD KMSNLLKIPG
IMITKTPARV YPLKEKAAML TGYVQNISAD ELKKLKTKGY SRDNVIGKAG LEKIYEKQLK
ATDGAEIYID SNYDKKIKTI AKKAPKNGKD VNLTIDTNIQ SSLYDEYKAD SGASVALNPK
TGAVLALVSA PSYNPNDFVL GMPSDKWNAL QNDANKPLLN RFKTTFAPGS TFKPITAAIA
LDAGKLNIDE DKKISGLKWQ ENSSWGNYFV TRDEAYSEPA NLVNALVHSD NIYFAKTALA
IGKDAFLSET KKLGIGQNLP FEYGLETSKI TSNGSIKDDI QLADSGYGQG EVLMNPVQLA
SIYTAFVNNG NIVAPYLNSD KGTQSKVLIK DAFKPDTINT IINDLTQVVS NPEGTGHGAY
MPDLPLAGKT GTAEIKKSQT DTTGTENGWF IAVNPSNPKL LVLEMYENVK GKGGSGYVVP
NVKSIFQQFG K
//
