ID Q8U0Z2_PYRFU Unreviewed; 634 AA.
AC Q8U0Z2;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Lon proteolytic domain-containing protein {ECO:0000259|PROSITE:PS51786};
GN OrderedLocusNames=PF1438 {ECO:0000313|EMBL:AAL81562.1};
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497 {ECO:0000313|EMBL:AAL81562.1, ECO:0000313|Proteomes:UP000001013};
RN [1] {ECO:0000313|EMBL:AAL81562.1, ECO:0000313|Proteomes:UP000001013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000313|Proteomes:UP000001013};
RX PubMed=10430560;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; AE009950; AAL81562.1; -; Genomic_DNA.
DR RefSeq; WP_011012585.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U0Z2; -.
DR STRING; 186497.PF1438; -.
DR MEROPS; S16.A12; -.
DR PaxDb; 186497-PF1438; -.
DR GeneID; 41713248; -.
DR KEGG; pfu:PF1438; -.
DR PATRIC; fig|186497.12.peg.1500; -.
DR eggNOG; arCOG01937; Archaea.
DR HOGENOM; CLU_027628_0_0_2; -.
DR OrthoDB; 15525at2157; -.
DR PhylomeDB; Q8U0Z2; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR027552; CGP_CTERM.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR04288; CGP_CTERM; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF05362; Lon_C; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Reference proteome {ECO:0000313|Proteomes:UP000001013};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 28..231
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 634 AA; 69926 MW; 18F04267A50F9A98 CRC64;
MRGKILSFLI VLTLLALPTT AQCPSLGRTV VLKAPAVSMT STGEMIGVPT EFVITVAPGS
GHVYVETWPL TEVDMQASAR LAAEIAGVVT GKDMSKYDVF IQVRADSPII GGPSAGGTMT
VGIIAALMGW DVRSDVMMTG MINPDGSIGP VGGILEKASA AHQAGAKIFL IPKGQRIQVV
TETQKKQIGP ITQITTTQRK VDVVEYAQER WGLKVIEISD IYEAVYYFTG HKLEKPQPPQ
NVVISTSFLE GEAKSDYEET LQYYNTISNK LKNSEVGYTT YSYLKAALDN AKSTLDNAKN
ALDSGKYYTA MSLSFQARIV IRHVDWYIDL YEGKDIEDIF SEVKDEIDRI ESYISNLTIR
GVTMLQAVAA AETRIEEAKE YLKEAQISYY NQDYWNAIGD AAYSYERART AELWAELGEK
YGRGEEISRE AIKKAARTQL DNARLIVTYI TSMFGEQNLQ DLVDTLNKGE AYYEDGKYSA
ALFSAMEARI RGEVILDTIG IDNVTVLKEK LEDIKESAKG AIALAQSGGT IPLLSMAYYE
FAESYEAKGD LEDLITAMIF YQYARETAMI FVSWKSQENT EVSTETEIIT TSTTTSTSTQ
TTTTQQTTTT TEQICGPGVL VALSLLGLVF RRRF
//
