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Database: UniProt/TrEMBL
Entry: Q31JA9_THICR
LinkDB: Q31JA9_THICR
Original site: Q31JA9_THICR 
ID   Q31JA9_THICR            Unreviewed;       323 AA.
AC   Q31JA9;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   11-JUN-2014, entry version 66.
DE   RecName: Full=Proline iminopeptidase;
DE            EC=3.4.11.5;
GN   OrderedLocusNames=Tcr_0168;
OS   Thiomicrospira crunogena (strain XCL-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XCL-2;
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J.,
RA   Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R.,
RA   Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A.,
RA   Freyermuth S.K., Harmer T.L., Hauser L.J., Huegler M., Kerfeld C.A.,
RA   Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L.,
RA   Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z.,
RA   Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T.,
RA   Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E.,
RA   Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira
RT   crunogena XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal proline from a peptide.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
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DR   EMBL; CP000109; ABB40764.1; -; Genomic_DNA.
DR   RefSeq; YP_390438.1; NC_007520.2.
DR   ProteinModelPortal; Q31JA9; -.
DR   SMR; Q31JA9; 7-314.
DR   STRING; 317025.Tcr_0168; -.
DR   MEROPS; S33.001; -.
DR   EnsemblBacteria; ABB40764; ABB40764; Tcr_0168.
DR   GeneID; 3762479; -.
DR   KEGG; tcx:Tcr_0168; -.
DR   PATRIC; 23972206; VBIThiCru83387_0175.
DR   eggNOG; COG0596; -.
DR   HOGENOM; HOG000171480; -.
DR   KO; K01259; -.
DR   OMA; FERWMVV; -.
DR   OrthoDB; EOG6BPDDC; -.
DR   BioCyc; TCRU317025:GHE8-168-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   InterPro; IPR005944; Pro_iminopeptidase.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF006431; Pept_S33; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01249; pro_imino_pep_1; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Complete proteome; Hydrolase; Protease.
FT   ACT_SITE    114    114       Nucleophile (By similarity){EA2}.
FT   ACT_SITE    269    269       By similarity{EA2}.
FT   ACT_SITE    297    297       Proton donor (By similarity){EA2}.
SQ   SEQUENCE   323 AA;  36847 MW;  301CBA25306FBA70 CRC64;
     MMTLDQILYP PIKPYSEHSL QVDNTHSLYI EESGNPLGLP VLFIHGGPGG GTTPMQRCFF
     NPDEYRIILF DQRGCGKSRP HACLTNNTTA HLIEDIEKIR RHLDIDRWVL FGGSWGSTLS
     LLYAEAYPER VISMVLRGIF LCREEDTRWF YQEGANRFYP NYWQDFIAPV PEEKRDDMIG
     AYYELLTSEN EIARMSAAEA WSVWEGRTST LKADKDLVNH FGDPYHALAM ARIECHYFKY
     KAFIEPNQIL DNIGYIQKIP TQIIQGRYDM VCPVNQAYAL SQAMPNAQLI ICDHAGHSAL
     ELEIAQALVG ATDQIYLDAD ISP
//
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