(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWK9_RUEPO

ID   Q5LWK9_RUEPO            Unreviewed;       316 AA.
AC   Q5LWK9;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 99.
DE   RecName: Full=Proline iminopeptidase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE            Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE            EC=3.4.11.5 {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN   Name=pip {ECO:0000313|EMBL:AAV93397.1};
GN   OrderedLocusNames=SPO0066 {ECO:0000313|EMBL:AAV93397.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93397.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93397.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93397.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.;
CC         EC=3.4.11.5; Evidence={ECO:0000256|PIRNR:PIRNR006431,
CC         ECO:0000256|RuleBase:RU003421};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006431}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421}.
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DR   EMBL; CP000031; AAV93397.1; -; Genomic_DNA.
DR   STRING; 246200.SPO0066; -.
DR   ESTHER; silpo-q5lwk9; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   EnsemblBacteria; AAV93397; AAV93397; SPO0066.
DR   KEGG; sil:SPO0066; -.
DR   eggNOG; ENOG4108HGY; Bacteria.
DR   eggNOG; COG0596; LUCA.
DR   HOGENOM; HOG000171480; -.
DR   KO; K01259; -.
DR   OMA; PDKWERF; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR43722; PTHR43722; 1.
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;
DR   PRODOM; Q5LWK9.
DR   SWISS-2DPAGE; Q5LWK9.
KW   Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431,
KW   ECO:0000256|RuleBase:RU003421, ECO:0000313|EMBL:AAV93397.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006431,
KW   ECO:0000256|RuleBase:RU003421, ECO:0000313|EMBL:AAV93397.1};
KW   Protease {ECO:0000256|PIRNR:PIRNR006431,
KW   ECO:0000256|RuleBase:RU003421};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT   DOMAIN       36    294       AB hydrolase-1. {ECO:0000259|Pfam:
FT                                PF00561}.
FT   ACT_SITE    110    110       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006431-1}.
FT   ACT_SITE    264    264       {ECO:0000256|PIRSR:PIRSR006431-1}.
FT   ACT_SITE    292    292       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006431-1}.
SQ   SEQUENCE   316 AA;  35393 MW;  04C2B8A1AF79228B CRC64;
     MQYLHPPIEP FDQRMLDVGQ GHRIYVEQSG NPNGIPVVVL HGGPGGGCSP AMRRYFDPSV
     YRVILFDQRG CGRSRPHASV TDNTTWHLVA DIERIRKTLE IDSWIAFGGS WGATLALIYA
     QTHPDRVTHL VLRGVFLMTQ AELDWFYGGG AGRFWPEPWS RFAALIPENE RGDMIAAYHK
     RLFSGDMAQE IRYARAWSAW ENALASIQSN GTTGESPGDY ARAFARLENH YFINDGFLEF
     DGQILANMGR ISHIPGHIVQ GRYDMICPPN SAWKLSELWP NADLRMIRNA GHALSEPGIS
     AELVRIMDAI AEEVTA
//

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