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Database: UniProt
Entry: A5FWZ0_ACICJ
LinkDB: A5FWZ0_ACICJ
Original site: A5FWZ0_ACICJ 
ID   A5FWZ0_ACICJ            Unreviewed;       457 AA.
AC   A5FWZ0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:ABQ30122.1};
DE            EC=3.4.21.102 {ECO:0000313|EMBL:ABQ30122.1};
GN   OrderedLocusNames=Acry_0903 {ECO:0000313|EMBL:ABQ30122.1};
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30122.1, ECO:0000313|Proteomes:UP000000245};
RN   [1] {ECO:0000313|EMBL:ABQ30122.1, ECO:0000313|Proteomes:UP000000245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30122.1,
RC   ECO:0000313|Proteomes:UP000000245};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; CP000697; ABQ30122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5FWZ0; -.
DR   STRING; 349163.Acry_0903; -.
DR   MEROPS; S41.004; -.
DR   KEGG; acr:Acry_0903; -.
DR   eggNOG; COG0793; Bacteria.
DR   HOGENOM; CLU_017295_1_2_5; -.
DR   Proteomes; UP000000245; 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   NCBIfam; TIGR00225; prc; 1.
DR   PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 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|RuleBase:RU004404, ECO:0000313|EMBL:ABQ30122.1};
KW   Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ABQ30122.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}.
FT   DOMAIN          90..158
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   457 AA;  49117 MW;  43DFE779674CE5C9 CRC64;
     MKLRTSLLIT ATFAVGIGVG MVAPAVHDAL AGVRQSDETY RQLGLFENIF QRIRADYVVP
     EPSKKLIYDA MNGMLTGLDP HSAYMNAQQY KDMKAETSGQ FGGLGIEVTE AGGFIKVITP
     IDGTPAAKAG IKPGDLIVAI DGKPMVGVTL DKAVDRMRGP AGSKIDITIK RPGVDKPVHV
     TLTRAIIHVH AVKTALYGDV GYLRLASFSE NANRDIRRGV AKLKAESHGK VDAYILDLRN
     NPGGLLDQGI AVADDFLNTG EIVSTHGRHQ SDDQVWYAHD GDITGGKPIV VLVNSGTASA
     AEIVSAALQQ NRRAVVMGTR TFGKGSVQTI FTIPGHGALR MTTALYYTPS GKSLQDYGVE
     PDLVVHETNN PKDHFPKIRE SNMPHAFRNP SGLKAPILPP KLVLPAVAKT IAPRPPASWP
     KFEPKHPNTD YQLQMALKLV RAMATNRVGA SQADVAH
//
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