ID A0A1B4XEH9_9GAMM Unreviewed; 263 AA.
AC A0A1B4XEH9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN ORFNames=SCL_0863 {ECO:0000313|EMBL:BAV33183.1};
OS Sulfuricaulis limicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Sulfuricaulis.
OX NCBI_TaxID=1620215 {ECO:0000313|EMBL:BAV33183.1, ECO:0000313|Proteomes:UP000243180};
RN [1] {ECO:0000313|EMBL:BAV33183.1, ECO:0000313|Proteomes:UP000243180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA5 {ECO:0000313|EMBL:BAV33183.1,
RC ECO:0000313|Proteomes:UP000243180};
RA Miura A., Kojima H., Fukui M.;
RT "Complete genome sequence of a sulfur-oxidizing gammaproteobacterium strain
RT HA5.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
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}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; AP014879; BAV33183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B4XEH9; -.
DR KEGG; slim:SCL_0863; -.
DR InParanoid; A0A1B4XEH9; -.
DR Proteomes; UP000243180; 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; cd07331; M48C_Oma1_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000243180};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..263
FT /note="Peptidase M48 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008572325"
FT DOMAIN 67..247
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 263 AA; 28852 MW; 096A58643930643F CRC64;
MKIMRQRMIM MPAGAVLVTV LMVACATVPE TGRSQLQLVS PAQETQLGFQ EFEKLKKSTP
ISKDAAATAQ LQRVGKRIAA IAPLPNAQWE FVLFDQPNTP NAFCLPGGKV GVFSGILPIT
KDDAGLATVV GHEVAHAVAR HGAERMSEGT LFQILEELAL GRSSPATRQV VQQAYGLGLA
LPHSRKQELE ADHLGLLYMA RAGYQPREAL GFWKRFAEYK NKNGGGKQIE FLSTHPLDDQ
RIRQIEGLIP QAEMEYRKPA NTP
//
