ID F2NF13_DESAR Unreviewed; 447 AA.
AC F2NF13;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:AEB08353.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:AEB08353.1};
GN OrderedLocusNames=Desac_0466 {ECO:0000313|EMBL:AEB08353.1};
OS Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC Bacteria; Thermodesulfobacteriota; Desulfobaccia; Desulfobaccales;
OC Desulfobaccaceae; Desulfobacca.
OX NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB08353.1, ECO:0000313|Proteomes:UP000000483};
RN [1] {ECO:0000313|EMBL:AEB08353.1, ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RX PubMed=21886866;
RA Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of the acetate-degrading sulfate reducer
RT Desulfobacca acetoxidans type strain (ASRB2).";
RL Stand. Genomic Sci. 4:393-401(2011).
RN [2] {ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179}.
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DR EMBL; CP002629; AEB08353.1; -; Genomic_DNA.
DR RefSeq; WP_013705466.1; NC_015388.1.
DR AlphaFoldDB; F2NF13; -.
DR STRING; 880072.Desac_0466; -.
DR KEGG; dao:Desac_0466; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_1_1_7; -.
DR OMA; ISIASCH; -.
DR Proteomes; UP000000483; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR PANTHER; PTHR32060:SF30; CARBOXY-TERMINAL PROCESSING PROTEASE CTPA; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEB08353.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AEB08353.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000483};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..447
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003282589"
FT DOMAIN 88..148
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 350..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 49110 MW; DF89DAFA91C4AA23 CRC64;
MWVFIVSLFF FGVLCCGSGP PAAATSSEAY AQLRLLVEAL YEIDQKYVTE KQDRDLIYGA
IRGMVSSLDA NSSFLSPSEY QEIQAGVKQP EASAGMELSI KDNILTVVSP IEGGPAWRTG
IKAGDHILKI NNQTTRNLTP LEAVKKLQGP PGTKVKLQLI RNGFVKPLDL ELTLEKLAVP
LVAHYQLEEG YHYLRLRSPQ EGAAAELQQI LRSIQANASP KKGLILDLRN TAGGRPDDAR
RIASSFLGND VIYIVKGRHS EQKQIVKGLK ECLVLKNKLP LVILVDHGTA QAAEVVTGAL
QAQWGALLLG YKTFGECGVV QTFPLKDGSA LVINVAFCYT PKDLLIQGRG LEPDLPGPKK
DPEEQPVRED SKDQEKPRNL PDVHEIMQDP LVHQALFQLK NWGSGRAIQS PGERSLKKNQ
AACFHSEEQE ITKISILGDQ EHSLFQA
//