ATP23_BOTFB
ID ATP23_BOTFB Reviewed; 244 AA.
AC A6SSS5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Mitochondrial inner membrane protease atp23;
DE EC=3.4.24.-;
GN Name=atp23; ORFNames=BC1G_15820;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Has a dual role in the assembly of mitochondrial ATPase. Acts
CC as a protease that removes N-terminal residues of mitochondrial ATPase
CC CF(0) subunit 6 at the intermembrane space side. Also involved in the
CC correct assembly of the membrane-embedded ATPase CF(0) particle,
CC probably mediating association of subunit 6 with the subunit 9 ring (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Intermembrane side. Note=Associates loosely with the inner
CC membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M76 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN23647.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH477043; EDN23647.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001545641.1; XM_001545591.1.
DR AlphaFoldDB; A6SSS5; -.
DR MEROPS; M76.002; -.
DR VEuPathDB; FungiDB:Bcin16g01380; -.
DR OrthoDB; 1288109at2759; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR019165; Peptidase_M76_ATP23.
DR PANTHER; PTHR21711; PTHR21711; 1.
DR Pfam; PF09768; Peptidase_M76; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion;
KW Mitochondrion inner membrane; Protease.
FT CHAIN 1..244
FT /note="Mitochondrial inner membrane protease atp23"
FT /id="PRO_0000330056"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 244 AA; 28756 MW; 9F79DA1833AE5DF5 CRC64;
MSSSEGNKPP LVPDSTKESE PQFDPTARTR NWFSILLGTM PPSHQILYRE DQYARHEKRD
CDRCEEWRDY NLKYSPIVIF MQKNIRDLNG KLDADNIRCR RCPTRITEDG KTVRQGGGFS
PEHGIQLCAN EMRDSKHVED TLAHEMVHAW DHLRWKVDWG DLRHAACSEI RAASLSGECR
WAREFWTRNN YRVTQQHQDC VRRRAVKSVL ARPWCKDDVQ AVRVVNEVWD SCYSDTRPFD
EIYK