ID   A0A0G3XCM3_9SPHN        Unreviewed;       451 AA.
AC   A0A0G3XCM3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Putative Zn-dependent protease {ECO:0000313|EMBL:AKM08349.1};
DE   Flags: Precursor;
GN   ORFNames=AM2010_2292 {ECO:0000313|EMBL:AKM08349.1};
OS   Pelagerythrobacter marensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Pelagerythrobacter.
OX   NCBI_TaxID=543877 {ECO:0000313|EMBL:AKM08349.1, ECO:0000313|Proteomes:UP000037643};
RN   [1] {ECO:0000313|EMBL:AKM08349.1, ECO:0000313|Proteomes:UP000037643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 22370 {ECO:0000313|EMBL:AKM08349.1,
RC   ECO:0000313|Proteomes:UP000037643};
RA   Kim K.M.;
RL   Submitted (JUN-2015) 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; CP011805; AKM08349.1; -; Genomic_DNA.
DR   RefSeq; WP_047807190.1; NZ_LMVG01000002.1.
DR   AlphaFoldDB; A0A0G3XCM3; -.
DR   STRING; 543877.AM2010_2292; -.
DR   KEGG; amx:AM2010_2292; -.
DR   PATRIC; fig|543877.4.peg.2326; -.
DR   OrthoDB; 9814887at2; -.
DR   Proteomes; UP000037643; 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, ECO:0000313|EMBL:AKM08349.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037643};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..451
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002562424"
FT   DOMAIN          33..223
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   451 AA;  48639 MW;  C08AC573802F20E9 CRC64;
     MHLIARILAL VAALSLAAQP VAAQSILRDA ETEALLDEMA APLVEAAGLQ PGNVDIVLIN
     DSSINAFVAG GQAVYIHTGL IDAADTANEV QGVIAHELGH ITGGHIIRHG EGASAATNIS
     LLSLLLGVGA ALAGAGEAAM GVMMAGQQAA LGKYLAFSRV QESSADAAGA EYLSKAGISG
     RGSLAFFGKL QNQEFRYGYS QSDEAGFART HPLSGDRIAR LREVYHTDPA WETPDDAELQ
     RRFERVKAKL FGYQQTPQRT MQAYPETMTG IPARYARAYA WHKDAQMDRA LAETDALLSA
     APDDPYFLEL KGQILLESGQ PQAALAPLRR ASELTRNQPL IASMFGHALI ATEDKDHYEE
     AERILRAAVG RDRLNPFAWY QLGVVYAARG DMPRARLASA EQQVMSRQYA MAIRSAQAAE
     AGLPEGSPDW IRAQDIALQA RAALERERER R
//