ID A1S152_THEPD Unreviewed; 628 AA.
AC A1S152;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Peptidase S16, lon domain protein {ECO:0000313|EMBL:ABL79182.1};
GN OrderedLocusNames=Tpen_1787 {ECO:0000313|EMBL:ABL79182.1};
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL79182.1, ECO:0000313|Proteomes:UP000000641};
RN [1] {ECO:0000313|Proteomes:UP000000641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX PubMed=18263724; DOI=10.1128/JB.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000505; ABL79182.1; -; Genomic_DNA.
DR RefSeq; WP_011753447.1; NC_008698.1.
DR AlphaFoldDB; A1S152; -.
DR STRING; 368408.Tpen_1787; -.
DR EnsemblBacteria; ABL79182; ABL79182; Tpen_1787.
DR GeneID; 4601931; -.
DR KEGG; tpe:Tpen_1787; -.
DR eggNOG; arCOG01937; Archaea.
DR HOGENOM; CLU_027628_0_0_2; -.
DR OrthoDB; 15525at2157; -.
DR Proteomes; UP000000641; 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:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
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 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 PRINTS; PR00830; ENDOLAPTASE.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000641}.
FT DOMAIN 49..237
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 570..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 67296 MW; CD068D7DBAE1EEB0 CRC64;
MLEKKFLGLP LALLVALSAV VVAASPPTAQ LKVIGSAWIL APAVAQTESG LVGSATNISV
FVTEGWGDVY VSTYSLTQED FQGAATAAAR VVTRLLGLNF SQYNYYFKVQ GDAVIVGGPS
AGVAMAVAVY SALTGKPINR TVFVTGMISP DGTVGPVGGV FEKAQAVAQA GAKVFLVPPG
QSIVTQYQTV ERKIGPFRLY TTQPVTVNLT EYAYKNWHLR VVEISTLSEA LRYFFGVSVA
RPPLGKPYLS ADTREKIASV KSSLTSLARK ELGEAYSYVN SSRLTQLGKS TLKSYLDRYA
KSYLDSATRA EGISSIPLLT SSIAVSRWIK LLVDYYSGLQ LDQQVQEVSD RLSRLAGAVE
DSAPRSIGEI NALILATDKV IHALKLFNES AAAWSSDPAT ALQKLAYSSA LLDEAENWLS
GIPRGGGIQA SQAAATYLSV ARSTWPYIYS VLSEAGGDLT LIDAASAYYQ ISARLYSSRK
PLLAAVAAAR SVALAEAAML YFQVQASGKD PYSGVSLENA LSVASATSDM LVTVYYINQS
YGAELRDSLA YLKLGSQLGQ LTLDLARVKP GQPAETQKTP SAPTQPEQPP QKPSQPGKSL
TDWLQEILLR ISLFIESIVD WFRRLLGK
//
