ID A0A0J6NRA5_9NEIS Unreviewed; 272 AA.
AC A0A0J6NRA5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:KMN83312.1};
GN ORFNames=VK98_03620 {ECO:0000313|EMBL:KMN83312.1};
OS Chromobacterium sp. LK11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN83312.1, ECO:0000313|Proteomes:UP000036114};
RN [1] {ECO:0000313|EMBL:KMN83312.1, ECO:0000313|Proteomes:UP000036114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LK11 {ECO:0000313|EMBL:KMN83312.1,
RC ECO:0000313|Proteomes:UP000036114};
RA Chan X.Y.;
RT "Draft genome of Chromobacterium aquaticum LK11.";
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMN83312.1}.
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DR EMBL; LDUR01000006; KMN83312.1; -; Genomic_DNA.
DR RefSeq; WP_048412725.1; NZ_LDUR01000006.1.
DR AlphaFoldDB; A0A0J6NRA5; -.
DR STRING; 1628212.VK98_03620; -.
DR PATRIC; fig|1628212.3.peg.4179; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000036114; Unassembled WGS sequence.
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:UP000036114};
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..272
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005279039"
FT DOMAIN 75..258
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 272 AA; 29046 MW; F3278A62AF93150D CRC64;
MKSFWSKTLA GLLVAAALAG CAQVNTTQGG AVGVSRGQTM LLSSQEVEQM SAKSYAQQLG
KSRAAGQLNA DAAMTARVRK ISQRLIAQAP VFRPDAAKWR WEVNVMRNDE PNAYAMAGGK
IMVYSGLITK LKLSDAELAA VIGHEISHAL REHSRESMSQ AYAQQVGLSL VGAVAGLRQS
QMDMAAMAAD VALSKPNSRT MESEADIMGL ELMARAGYDP NAAVNVWNKM QAAGNGGGVE
FLSTHPSGPT RIRDLQQRIP QVMPLYQAAK KA
//