ID J2KFE2_9BURK Unreviewed; 280 AA.
AC J2KFE2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:EJL78935.1};
GN ORFNames=PMI15_04226 {ECO:0000313|EMBL:EJL78935.1};
OS Polaromonas sp. CF318.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1144318 {ECO:0000313|EMBL:EJL78935.1, ECO:0000313|Proteomes:UP000007275};
RN [1] {ECO:0000313|EMBL:EJL78935.1, ECO:0000313|Proteomes:UP000007275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF318 {ECO:0000313|EMBL:EJL78935.1,
RC ECO:0000313|Proteomes:UP000007275};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL78935.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKIV01000135; EJL78935.1; -; Genomic_DNA.
DR RefSeq; WP_007873865.1; NZ_AKIV01000135.1.
DR AlphaFoldDB; J2KFE2; -.
DR PATRIC; fig|1144318.3.peg.4077; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000007275; 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.
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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT DOMAIN 86..266
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 238..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 280 AA; 29895 MW; 2F9F408E22FA5375 CRC64;
MCFLCDAKHS AWPGRRAFLL AAAGTAATAA TTPLRAQVDV GPASQLRNLV PADEIEGAAT
QEYSKLLAEA RAKGALAPQG HPQLQRLRAI AAKLVPQTAQ WNDRARQWRW EVNLLGSKQI
NAFCMPGGKI AFYTGILDQL KLTDDEAAMI MGHEMAHALR EHARARIAKS QGTGTLLSLG
AQLLGWGQVG DLAASIGTQL LTLRFSREDE TDADLVGLEL AARGGYNPQA AVSLWEKMGQ
AGGGSSGPSF LSTHPSGPER IQQLQANVPK VQGLYQRARG
//
