ID L0KWA8_METHD Unreviewed; 311 AA.
AC L0KWA8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Archaeal serine protease {ECO:0000313|EMBL:AGB49416.1};
DE Flags: Precursor;
GN OrderedLocusNames=Metho_1186 {ECO:0000313|EMBL:AGB49416.1};
OS Methanomethylovorans hollandica (strain DSM 15978 / NBRC 107637 / DMS1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanomethylovorans.
OX NCBI_TaxID=867904 {ECO:0000313|EMBL:AGB49416.1, ECO:0000313|Proteomes:UP000010866};
RN [1] {ECO:0000313|Proteomes:UP000010866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15978 / NBRC 107637 / DMS1
RC {ECO:0000313|Proteomes:UP000010866};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Methanomethylovorans hollandica DSM
RT 15978.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003362; AGB49416.1; -; Genomic_DNA.
DR RefSeq; WP_015324582.1; NC_019977.1.
DR AlphaFoldDB; L0KWA8; -.
DR STRING; 867904.Metho_1186; -.
DR GeneID; 14406995; -.
DR KEGG; mhz:Metho_1186; -.
DR HOGENOM; CLU_079274_0_0_2; -.
DR OMA; QACPAGM; -.
DR OrthoDB; 15525at2157; -.
DR Proteomes; UP000010866; 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; 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 ECO:0000313|EMBL:AGB49416.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010866};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 145..310
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 311 AA; 34370 MW; DCE8D5CAEEB39FB3 CRC64;
MTYATKHKVC IFLLIISLTA NLYLLALQQP VQDEQVRILQ DSINSLEAEN EILNAQISQD
NVSLQSYASQ IDYYRQRLNE IEYSMGLSSD GYEGTASLQA PAVYQSIEEY IDGPFIRQTV
IEKGSMMDIS VEIDPGKGRV LVETKPLMGV VFQDAANTAV FLAQNITNSN LMASDTIFSI
TAADEVPSVD GPSAGALMTL LMISALKNEQ LNDSVTMTGT IDQYGNVGAV GGIVEKAEAA
KDNGKELFLL PRENRRLVQY SYVEKNIGGF SIIERRPEII DAKTHIEETI GIRVEYVDSI
HDIIRYAVEI N
//