ID A0A3A3FMT9_9BURK Unreviewed; 298 AA.
AC A0A3A3FMT9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=M48 family peptidase {ECO:0000313|EMBL:RJF97502.1};
GN ORFNames=D3871_02370 {ECO:0000313|EMBL:RJF97502.1};
OS Noviherbaspirillum saxi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=2320863 {ECO:0000313|EMBL:RJF97502.1, ECO:0000313|Proteomes:UP000265955};
RN [1] {ECO:0000313|Proteomes:UP000265955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1R23-30 {ECO:0000313|Proteomes:UP000265955};
RA Zhu H.;
RL Submitted (SEP-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}.
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:RJF97502.1}.
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DR EMBL; QYUO01000001; RJF97502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A3FMT9; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000265955; 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 Reference proteome {ECO:0000313|Proteomes:UP000265955};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..298
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017309292"
FT DOMAIN 81..264
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 298 AA; 32135 MW; C294850192A0768A CRC64;
MNRHTPLTLT LAALVSISPL VMAKDEVSSD GVKVDKMSPL RNLVPEEQLE AAASEQYVGI
KQQANQHKAL AADDHPEVQR LRAIARKLIP HAVRWNDRAS KWQWEVNLIG SKEINAFCMP
GGKIAFFSGI LSNLKLTDDE VAIVMGHEIA HALREHGRER VAKSGLASAG AKIAGIGLSA
LLGVDPNLAT AATGGIANLT MLKFSRDDET EADLVGLDIV ARAGYDPRAG IALWQKMGMI
SKNAPPQWFS THPAGKSRIA EMQKHMPSVV PLYAKAKGVQ PTSLPPYESN VKGIAPIR
//
