ID E4NKX5_HALBP Unreviewed; 711 AA.
AC E4NKX5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN OrderedLocusNames=Hbor_15570 {ECO:0000313|EMBL:ADQ67127.1};
OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS KCTC 4070 / PR3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ67127.1, ECO:0000313|Proteomes:UP000006663};
RN [1] {ECO:0000313|EMBL:ADQ67127.1, ECO:0000313|Proteomes:UP000006663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC {ECO:0000313|Proteomes:UP000006663};
RX PubMed=21304651; DOI=10.4056/sigs.23264;
RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Halogeometricum borinquense type strain
RT (PR3).";
RL Stand. Genomic Sci. 1:150-159(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228}.
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DR EMBL; CP001690; ADQ67127.1; -; Genomic_DNA.
DR AlphaFoldDB; E4NKX5; -.
DR STRING; 469382.Hbor_15570; -.
DR ESTHER; halbp-e4nkx5; S9N_PPCE_Peptidase_S9.
DR MEROPS; S09.076; -.
DR KEGG; hbo:Hbor_15570; -.
DR eggNOG; arCOG01647; Archaea.
DR HOGENOM; CLU_011290_1_1_2; -.
DR Proteomes; UP000006663; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADQ67127.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006663};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..440
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 506..708
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 78742 MW; E99EE33C3FAFC645 CRC64;
MISALSDRHS RGDGFRNPEI LVTICSRTRM DSPPETDQRD TGYTLHDDDI DDPYLWLEET
DDDVSAWTAA QNDYADDYLD SLDIRESLRP RFEDLARTTT YMPVKARQNG YFQRVRDADA
DHPVLTFRPG LNEDRRVLGD PNEMSDDGSV SVDWYVPNPD GSLVAYGVAE GGDEQYDVRV
LETESGETAE ELTDVGRTGP WCFGWTDDGF YYLTTGSVGD GGQLEKEVCF HEIGTDPADD
WTLADEFSTQ TWPLVETDAE SDYVILGHTE GWERTDLYYA ELGSDELHPL VVGEDALFEP
TLDGNDVYVN TSLDASNYRV VSVSLDAVDP SASPTDVGES STDPNKPFET VVAERDDAIA
QELDVIGDRI VVKYLRDAVH ELVVFDADGE QDETVPLPGR GSVASFGGED DLFFTYESFT
EPPSIRRYAF GADETTVVDQ PDISTETDLT VTQDWFASAD GTEVPAFVVR RSDLECDGDN
PAVLYGYGGF ENSLTPFFGE FFLPFLESGG VLAVANLRGG GEFGESWHHA GRREHKQRVF
DDFFAAAEHL VENGYTSTER LACFGGSNGG LLVGASITQR PDLFAAAVCK VPLLDMLRFH
TSLLGETWTT EYGSPDDPEA YEYIREYSPY HNVEERAYPA VLFTTGESDS RVDPFHARKM
AARMQAAQSG ADPILLKTRS QTGHGSGKPV SKVVEENLDE WSFLGDQLDA F
//