ID A0A3S9MYF9_9FLAO Unreviewed; 275 AA.
AC A0A3S9MYF9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=M48 family peptidase {ECO:0000313|EMBL:AZQ44285.1};
GN ORFNames=EJ995_08570 {ECO:0000313|EMBL:AZQ44285.1};
OS Nonlabens ponticola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=2496866 {ECO:0000313|EMBL:AZQ44285.1, ECO:0000313|Proteomes:UP000279600};
RN [1] {ECO:0000313|EMBL:AZQ44285.1, ECO:0000313|Proteomes:UP000279600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ115 {ECO:0000313|EMBL:AZQ44285.1,
RC ECO:0000313|Proteomes:UP000279600};
RA Choi H.S., Jung J.;
RT "Complete genome of Nonlabens sp. MJ115.";
RL Submitted (DEC-2018) 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; CP034549; AZQ44285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9MYF9; -.
DR KEGG; noj:EJ995_08570; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000279600; 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:UP000279600};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..275
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019293041"
FT DOMAIN 80..258
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 275 AA; 30118 MW; AC9B3554174BA468 CRC64;
MKITRISLVA AMLLLFSCKT NVFTGERTLN FVSNEQIFPA AFAQYDQVLE QSTVERETAE
ARMVKRVGQN IKVAAERWLN ALGHPEYLDG YNWEYNLIKD DQVNAWAMPG GKIAFYTGIL
PIAQEETGVA VIMGHEVAHA LANHGAQRMS RQQAASIVGT GVAVAASGRS QTTQQIIGQA
YGLGAQYGAI LPFSRKNEQE ADKIGLILTA IAGYDPDEGA RLWERMKANS AQNGQEAPPE
FLSTHPSYDT RIQNLRKLAP IAKAEAAKYG VTTFK
//
