ID A0A328B4G9_9CAUL Unreviewed; 466 AA.
AC A0A328B4G9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=M48 family peptidase {ECO:0000313|EMBL:RAK61465.1};
GN ORFNames=DJ021_17470 {ECO:0000313|EMBL:RAK61465.1};
OS Phenylobacterium hankyongense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1813876 {ECO:0000313|EMBL:RAK61465.1, ECO:0000313|Proteomes:UP000249842};
RN [1] {ECO:0000313|Proteomes:UP000249842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKS-05 {ECO:0000313|Proteomes:UP000249842};
RA Li X.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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 -!- 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:RAK61465.1}.
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; QFYP01000001; RAK61465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328B4G9; -.
DR OrthoDB; 9814887at2; -.
DR Proteomes; UP000249842; 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; cd07324; M48C_Oma1-like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF13432; TPR_16; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000249842};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..466
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016265322"
FT DOMAIN 38..230
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 466 AA; 50531 MW; 8EDB399A69B96E06 CRC64;
MVSTARSISR IALAVTLSAS LVLRAAPAAA QQGESLIRDT EIEQILHDDA DPIFRAAGID
PKTVQIALIG SKELNAFAGP GVMGVNTGLI LQTKNPNELQ GVIAHEVGHL AAGHSARSGE
MQHAGMVPFI LTMGLGVLAA IAGSGQAAAG LVGSAGYFGT LGAIGYSREQ ESRADQAGAT
LLEKAGLSGR GLAEFFDNFR YQEVFAEARR YRYFVDHPLS SDRIDALQSR VAAQPHYKEV
DGPEAIAEHE IMKAKLDGFI NPQVSIVKYA ETDKAYPARY ARAIAYYQMR EPDKALKLID
ALIEEQPDNP YLWELKGQVL FEFGRAKEAE APQRKSVALK PDAPLLRVNL GQTLIALDDK
AKVDEGVAEL RKALLKEGDN AVAWRLLAEA YDKRGDDGLA RLATAEYNFS IGDATQARIF
AMRAREKLAK DTPEWRRATD IVLTSKPSKD DLKDLAREGS ITSARH
//
