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Database: UniProt
Entry: D5SPX7_PLAL2
LinkDB: D5SPX7_PLAL2
Original site: D5SPX7_PLAL2 
ID   D5SPX7_PLAL2            Unreviewed;       394 AA.
AC   D5SPX7;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Dipeptidyl aminopeptidase/acylaminoacyl-peptidase-like protein {ECO:0000313|EMBL:ADG68352.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Plim_2527 {ECO:0000313|EMBL:ADG68352.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG68352.1, ECO:0000313|Proteomes:UP000002220};
RN   [1] {ECO:0000313|EMBL:ADG68352.1, ECO:0000313|Proteomes:UP000002220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC   {ECO:0000313|Proteomes:UP000002220};
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
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DR   EMBL; CP001744; ADG68352.1; -; Genomic_DNA.
DR   RefSeq; WP_013110783.1; NC_014148.1.
DR   AlphaFoldDB; D5SPX7; -.
DR   STRING; 521674.Plim_2527; -.
DR   KEGG; plm:Plim_2527; -.
DR   eggNOG; COG1506; Bacteria.
DR   HOGENOM; CLU_699912_0_0_0; -.
DR   Proteomes; UP000002220; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type 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; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR22946; UNCHARACTERIZED; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:ADG68352.1};
KW   Hydrolase {ECO:0000313|EMBL:ADG68352.1};
KW   Protease {ECO:0000313|EMBL:ADG68352.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002220};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..394
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003076120"
FT   DOMAIN          202..299
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          23..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  42009 MW;  D8F3187E986F8D03 CRC64;
     MSGRFVIFSL AFLCIVHGCS SQAGKNPAGA DGSASEQKLQ VTEPQELASA APLATQDSPA
     TSDPLPTSDP QPQSQSARPE SSAASEAVVM TPAQPPAVNP QAAAGSPAAV TASPEAATNK
     FNEARKKLQT KIVSEIPRSG PPEVPPKSSQ FQLIRYTSPV GNLAAYVTRD PRDGKRHPAI
     IWITGGDSNE IGDVWSPADR DFDQSASAFR KAGIVMMFPS LRGGNNNPGV REGFLGEVDD
     ILAATDHLAK LPYVDPQQIY LGGHSTGGTL VMLVGAASDR YRAIFVLGPV AFANQYDGEY
     VYGDTSNRTE VVVRSPSFWL DSIQSPMYVI EGDTGGNWNT IRSMQKKNKN PQIHFLKIPR
     KTHFSVIGPV AEKLAPQIIA GQVTLTEEDA EAIK
//
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