ID Q0AQ50_MARMM Unreviewed; 453 AA.
AC Q0AQ50;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Peptidase M48, Ste24p {ECO:0000313|EMBL:ABI65587.1};
DE Flags: Precursor;
GN OrderedLocusNames=Mmar10_1295 {ECO:0000313|EMBL:ABI65587.1};
OS Maricaulis maris (strain MCS10).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI65587.1, ECO:0000313|Proteomes:UP000001964};
RN [1] {ECO:0000313|EMBL:ABI65587.1, ECO:0000313|Proteomes:UP000001964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10 {ECO:0000313|EMBL:ABI65587.1,
RC ECO:0000313|Proteomes:UP000001964};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
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DR EMBL; CP000449; ABI65587.1; -; Genomic_DNA.
DR RefSeq; WP_011643234.1; NC_008347.1.
DR AlphaFoldDB; Q0AQ50; -.
DR STRING; 394221.Mmar10_1295; -.
DR KEGG; mmr:Mmar10_1295; -.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_030556_2_0_5; -.
DR OrthoDB; 9814887at2; -.
DR Proteomes; UP000001964; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07324; M48C_Oma1-like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001964};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..453
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004168610"
FT DOMAIN 30..220
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 453 AA; 49685 MW; 9C6606D0A9DEBEB3 CRC64;
MSILKTVAAA CVFAVATYTP AFGQSLIRDT EIEHMLRDYA DPILVAAGLQ PADVDMYIVA
DPSLNAFVTG GQNIFLHTGI ILESGTPNQL KGVIAHETGH IAGAHLARVN DGIAAAQAPM
YVSLGLGVLA ALAGEGGAAG ALLASSQQFG ALSFMTYSRA QEASADQAGL QFMEATGQSA
QGLVQFFERF RYQEVMSNAR RYPYFRSHPL SSERIANLRG GATESPYYET LDGPEELARL
QRIQGKIYGF LAEPEFVFYR YPESDQSLPA RYARAVAYYH DARLERALEE IASLLAEEPE
NPYFHELHAQ MLFESGRPGQ AIAPNRRSVE LEPTAPLLRI NLATSLIATD DPDHLEEASQ
NLRVALDIEP DNGFAWYQLS IVHERNGDTA LAQLAIAEQS YAAGNRQRAH QFASRARTAL
EIGTPAWVRA TEIESVSLPT EAEMRQIRRQ QRN
//