ID M9RLN8_9RHOB Unreviewed; 439 AA.
AC M9RLN8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=TPR-repeat containing protein {ECO:0000313|EMBL:AGI71326.1};
GN ORFNames=OA238_c11450 {ECO:0000313|EMBL:AGI71326.1};
OS Octadecabacter arcticus 238.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391616 {ECO:0000313|EMBL:AGI71326.1, ECO:0000313|Proteomes:UP000004688};
RN [1] {ECO:0000313|EMBL:AGI71326.1, ECO:0000313|Proteomes:UP000004688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=238 {ECO:0000313|EMBL:AGI71326.1,
RC ECO:0000313|Proteomes:UP000004688};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
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; CP003742; AGI71326.1; -; Genomic_DNA.
DR RefSeq; WP_015494537.1; NC_020908.1.
DR AlphaFoldDB; M9RLN8; -.
DR STRING; 391616.OA238_c11450; -.
DR KEGG; oar:OA238_c11450; -.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_030556_2_0_5; -.
DR OrthoDB; 9814887at2; -.
DR Proteomes; UP000004688; 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; 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 SUPFAM; SSF48452; TPR-like; 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:UP000004688};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..439
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004102341"
FT DOMAIN 33..223
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 439 AA; 46711 MW; BFE3AFBFCE833917 CRC64;
MRLSVLSIFL SAAITLVSVA APAHAVNLIR DADIEHSLDQ LAAPILRAAG LNPNNVRILI
VNDSTMNAFV INERAIFIHS GLLQRVNSAG QLQSIIAHEA AHIANDHISR RLTNLRGANT
AAGFGIALAL AVAIASDSGA AAGGIAAGAA GAAQRQFFAH TRAEESAADQ SSVRFMLRAG
VDPASTAEVL ELFRGQEALS VSRQAPYART HPLTSDRIRA LRGLIAANPG NAAPNPNADF
WFARAQGKLS AFTQNPSWTL RRVRNDDSPV GLMRAAVAYH RQADANRAIQ TMQTLLAQYP
NDAYWYELFG QILLESRQAG PAVQAYQNAV ALNGDEPLIL AGYGRALLAL DTADSNARAV
TTLERARALD GQSSATLRDL GQAYARTNQP GLASLATAER YALQGRMDDA LVHATRGVDR
LARGSAPWQR AQDVLSAVQ
//
