GenomeNet

Database: UniProt
Entry: Q8EKM1_SHEON
LinkDB: Q8EKM1_SHEON
Original site: Q8EKM1_SHEON 
ID   Q8EKM1_SHEON            Unreviewed;       539 AA.
AC   Q8EKM1;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00012568};
DE            EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
GN   OrderedLocusNames=SO_0071 {ECO:0000313|EMBL:AAN53158.1};
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN53158.1, ECO:0000313|Proteomes:UP000008186};
RN   [1] {ECO:0000313|EMBL:AAN53158.1, ECO:0000313|Proteomes:UP000008186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1 {ECO:0000313|EMBL:AAN53158.1,
RC   ECO:0000313|Proteomes:UP000008186};
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA   Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA   Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001585};
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014299; AAN53158.1; -; Genomic_DNA.
DR   RefSeq; NP_715713.1; NC_004347.2.
DR   AlphaFoldDB; Q8EKM1; -.
DR   STRING; 211586.SO_0071; -.
DR   ESTHER; sheon-SO0071; Proline_iminopeptidase.
DR   PaxDb; 211586-SO_0071; -.
DR   KEGG; son:SO_0071; -.
DR   PATRIC; fig|211586.12.peg.71; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_025429_1_0_6; -.
DR   OMA; LNCAYWP; -.
DR   OrthoDB; 4510475at2; -.
DR   PhylomeDB; Q8EKM1; -.
DR   BioCyc; SONE211586:G1GMP-72-MONOMER; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   InterPro; IPR002410; Peptidase_S33.
DR   PANTHER; PTHR43798:SF27; HYDROLASE ALPHA/BETA HYDROLASE FOLD FAMILY; 1.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000313|EMBL:AAN53158.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008186}.
FT   DOMAIN          113..252
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          398..497
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          517..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  58590 MW;  B2FC3AF4EEDFD213 CRC64;
     MRDSMTHRKS HNASACVAIK RSNTGWHKRI STSKIIGLST LMLAMCSATV WASDKPTPPT
     TPTNTCYVEG VSDRLQCGFV TVPENPNQPD GKQIQVHYVV LPAVKNANHE EALLAIAGGP
     GQSAIDNAAS FNTVLNKVRQ QRDILLIDQR GTGRSNLLNC DAGPQSLLAF NDDNVDSLAE
     AQKCRDQLAG SDVTQYGSLN AVKDFEAVRA HLGYKKLHLY GISYGTRMAQ LYMRLYPEHL
     ATVTLDGIVP MQQSVLEIGS AIERGFDLLF KDCQETAACH AKFPELKAEF DQVVARLTEG
     PIMEQVHDPV TGEKTLLTMT RAKFYGAIRM ALYQTNVRAL VPHAIHQAAK GNYQPLLGLY
     ALTTDGAGMA MGMHASVVCG EDIHRITPAM REQAKTSYVG KTMLESLEAS CSVWKVPPVD
     ASFSEPIKSD IPTLLLSGEI DPATPPSWGE LAMEKLTNAK HFIAPYATHG VAYQSCANNL
     VAELVRTGSV KDLDGECLKK DVRRSFYLNA SSVEPLTTEA ATNSAKDKPK DKPSTGAKE
//
DBGET integrated database retrieval system