ID A8AAW9_IGNH4 Unreviewed; 552 AA.
AC A8AAW9;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Peptidase S16, lon domain protein {ECO:0000313|EMBL:ABU82071.1};
GN OrderedLocusNames=Igni_0889 {ECO:0000313|EMBL:ABU82071.1};
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591 {ECO:0000313|EMBL:ABU82071.1, ECO:0000313|Proteomes:UP000000262};
RN [1] {ECO:0000313|EMBL:ABU82071.1, ECO:0000313|Proteomes:UP000000262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125
RC {ECO:0000313|Proteomes:UP000000262};
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H.Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000816; ABU82071.1; -; Genomic_DNA.
DR RefSeq; WP_012123035.1; NC_009776.1.
DR AlphaFoldDB; A8AAW9; -.
DR STRING; 453591.Igni_0889; -.
DR GeneID; 5562020; -.
DR KEGG; iho:Igni_0889; -.
DR eggNOG; arCOG01937; Archaea.
DR HOGENOM; CLU_493163_0_0_2; -.
DR OrthoDB; 15525at2157; -.
DR PhylomeDB; A8AAW9; -.
DR Proteomes; UP000000262; 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:UP000000262}.
FT DOMAIN 40..228
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
SQ SEQUENCE 552 AA; 59594 MW; 0BA2275A8F8FDFA2 CRC64;
MKQLAALLIL TSLAFGLSQC YSQVRTVEVP VVGVSLGPGG EERGVVGTLQ VTVAYPGKGE
IYVASEPLTE VDTQGVARVA VLVASALAHK DWTKYDFFFK FRTPSVIVGG PSAGLAMTVA
AYSALTGTPL REDVAGTGTV GPDGVVGPVG GVYAKMVAAA KSGYKVFVVP KGEEVVTRKV
VETEPLPFGI VQRLRTEKVN LIEEGKRLGV EVVPAATAYD ALRVWLKGAE LPECKPDVRL
PGDVLRLMRE WKEHYLKLYE GARSEARRLT QESVALLSEA ERMARAAGEE KDPYEAVNYA
FTAAILAEEA KWYDEVALSG FRALVKLSDE VESKINEANA TIMNSLTYDV NKLDPLLTAA
TRVLKAYYFY HAALNSTDLG NIIYYLVLAK YYSEAAKTWI ALTSLEPPGP KADPEALWRD
ALALYSSAGE LFAYYTTIGS QVGAVPSREL EVAVGVYKEA NDMPAIYKLA ASTYLSALVT
YSLHTTYNIS SETMIDKVMA ALSCNAALAL DRGLKPYAAE IYYTSARASE GEAAFLYAAL
ASTHFLLLSL LA
//
