ID Q8TSP3_METAC Unreviewed; 305 AA.
AC Q8TSP3;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Lon proteolytic domain-containing protein {ECO:0000259|PROSITE:PS51786};
GN OrderedLocusNames=MA_0752 {ECO:0000313|EMBL:AAM04192.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM04192.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM04192.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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; AE010299; AAM04192.1; -; Genomic_DNA.
DR RefSeq; WP_011020797.1; NC_003552.1.
DR AlphaFoldDB; Q8TSP3; -.
DR STRING; 188937.MA_0752; -.
DR MEROPS; S16.012; -.
DR EnsemblBacteria; AAM04192; AAM04192; MA_0752.
DR GeneID; 1472644; -.
DR KEGG; mac:MA_0752; -.
DR HOGENOM; CLU_079274_0_0_2; -.
DR InParanoid; Q8TSP3; -.
DR OrthoDB; 15525at2157; -.
DR PhylomeDB; Q8TSP3; -.
DR Proteomes; UP000002487; 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; 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; SSF75704; Mitotic arrest deficient-like 1, Mad1; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Reference proteome {ECO:0000313|Proteomes:UP000002487};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 181..305
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 33..81
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 305 AA; 33154 MW; B32C772D897C73ED CRC64;
MKSKLLALIL VLSLVANAYF VFFYQAPVEG EQVQEMQERI NSLEKDNNRL ETQVSQNNQS
LQSYASQLDF YRERVFELEN NLQACPAGME GFATLQAPAV FQNVELEKSG PFVREVISEE
GTLLNISTET RSGKGRVLVQ TTPLMGVVFQ DAANTAVFVA QQETGVSLSG SDVIFSIASD
QEIPGVDGSS AGALMTLLTI SAINGTELND SITLTGTIDD EGNVGEIGGV FEKATAAEAG
GKTLFLLPRE NSELVTYKLV SRKIGGIDVV QRVPETVDAE EYIEENVGIN VEYVDTIEDV
LEYET
//
