(data stored in ACNUC7421 zone)

SWISSPROT: C6WGI9_ACTMD

ID   C6WGI9_ACTMD            Unreviewed;       214 AA.
AC   C6WGI9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 61.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000256|HAMAP-Rule:MF_00417};
DE            EC=3.4.19.3 {ECO:0000256|HAMAP-Rule:MF_00417};
DE   AltName: Full=5-oxoprolyl-peptidase {ECO:0000256|HAMAP-Rule:MF_00417};
DE   AltName: Full=Pyroglutamyl-peptidase I {ECO:0000256|HAMAP-Rule:MF_00417};
DE            Short=PGP-I {ECO:0000256|HAMAP-Rule:MF_00417};
DE            Short=Pyrase {ECO:0000256|HAMAP-Rule:MF_00417};
GN   Name=pcp {ECO:0000256|HAMAP-Rule:MF_00417};
GN   OrderedLocusNames=Amir_0336 {ECO:0000313|EMBL:ACU34305.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34305.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34305.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {ECO:0000256|HAMAP-Rule:MF_00417,
CC       ECO:0000256|SAAS:SAAS00791207}.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal pyroglutamyl group
CC       from a polypeptide, the second amino acid generally not being Pro.
CC       {ECO:0000256|HAMAP-Rule:MF_00417, ECO:0000256|PROSITE-
CC       ProRule:PRU10076, ECO:0000256|SAAS:SAAS00791216}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00417,
CC       ECO:0000256|SAAS:SAAS00719542}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00417,
CC       ECO:0000256|SAAS:SAAS00791206}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00417, ECO:0000256|SAAS:SAAS00791205}.
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DR   EMBL; CP001630; ACU34305.1; -; Genomic_DNA.
DR   RefSeq; WP_012782968.1; NC_013093.1.
DR   ProteinModelPortal; C6WGI9; -.
DR   STRING; 446462.Amir_0336; -.
DR   MEROPS; C15.001; -.
DR   EnsemblBacteria; ACU34305; ACU34305; Amir_0336.
DR   KEGG; ami:Amir_0336; -.
DR   eggNOG; ENOG4108KN7; Bacteria.
DR   eggNOG; COG2039; LUCA.
DR   HOGENOM; HOG000242641; -.
DR   KO; K01304; -.
DR   OMA; VCNHVFY; -.
DR   OrthoDB; POG091H07B8; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-HAMAP.
DR   CDD; cd00501; Peptidase_C15; 1.
DR   Gene3D; 3.40.630.20; -; 1.
DR   HAMAP; MF_00417; Pyrrolid_peptidase; 1.
DR   InterPro; IPR000816; Peptidase_C15.
DR   InterPro; IPR016125; Peptidase_C15-like.
DR   InterPro; IPR029762; PGP-I_bact-type.
DR   InterPro; IPR033694; PGPEP1_Cys_AS.
DR   InterPro; IPR033693; PGPEP1_Glu_AS.
DR   PANTHER; PTHR23402; PTHR23402; 1.
DR   Pfam; PF01470; Peptidase_C15; 1.
DR   PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR   PRINTS; PR00706; PYROGLUPTASE.
DR   SUPFAM; SSF53182; SSF53182; 1.
DR   TIGRFAMs; TIGR00504; pyro_pdase; 1.
DR   PROSITE; PS01334; PYRASE_CYS; 1.
DR   PROSITE; PS01333; PYRASE_GLU; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WGI9.
DR   SWISS-2DPAGE; C6WGI9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00417,
KW   ECO:0000256|SAAS:SAAS00791208};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00417,
KW   ECO:0000256|SAAS:SAAS00791211, ECO:0000313|EMBL:ACU34305.1};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00417,
KW   ECO:0000256|SAAS:SAAS00791203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Thiol protease {ECO:0000256|HAMAP-Rule:MF_00417,
KW   ECO:0000256|SAAS:SAAS00791212}.
FT   ACT_SITE     79     79       {ECO:0000256|HAMAP-Rule:MF_00417,
FT                                ECO:0000256|PROSITE-ProRule:PRU10076}.
FT   ACT_SITE    142    142       {ECO:0000256|HAMAP-Rule:MF_00417,
FT                                ECO:0000256|PROSITE-ProRule:PRU10077}.
FT   ACT_SITE    166    166       {ECO:0000256|HAMAP-Rule:MF_00417}.
SQ   SEQUENCE   214 AA;  22401 MW;  E1C8EED0C4AF2E4C CRC64;
     MDDPTVLITG FEPFGGERTN PSWDAVRELA ERDPSLIAVE LPCAFDASAR ALREAVERHR
     PDLVVCVGQA GGRSGVTPER VAINLADARI PDNDGAQPID VPVVEGGPAA YFTGLPVKAC
     VAALEEAGIP ASVSHTAGTF VCNHVFYALM HLVATDFPDL RGGFVHVPFA PEQVADREGV
     PSLEVSRTAD ALGLIVATCL STTDDLAIST GTLS
//

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