ID U3K751_FICAL Unreviewed; 636 AA.
AC U3K751;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Mitochondrial-processing peptidase subunit beta {ECO:0000256|ARBA:ARBA00020510};
DE EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299};
DE AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018};
GN Name=PMPCB {ECO:0000313|Ensembl:ENSFALP00000010855.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000010855.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000010855.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000010855.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal transit peptides from precursor proteins
CC imported into the mitochondrion, typically with Arg in position P2.;
CC EC=3.4.24.64; Evidence={ECO:0000256|ARBA:ARBA00001098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Heterodimer of PMPCA (alpha) and PMPCB (beta) subunits,
CC forming the mitochondrial processing protease (MPP) in which PMPCA is
CC involved in substrate recognition and binding and PMPCB is the
CC catalytic subunit. {ECO:0000256|ARBA:ARBA00011587}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR AlphaFoldDB; U3K751; -.
DR STRING; 59894.ENSFALP00000010855; -.
DR Ensembl; ENSFALT00000010899.2; ENSFALP00000010855.2; ENSFALG00000010410.2.
DR eggNOG; KOG0960; Eukaryota.
DR GeneTree; ENSGT00940000156608; -.
DR HOGENOM; CLU_009902_4_2_1; -.
DR Proteomes; UP000016665; Chromosome 1A.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:Ensembl.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF103; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT BETA; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT DOMAIN 220..365
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 371..555
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 69906 MW; E2A2313164E5EC3F CRC64;
MAAGGRVWGY GEPRPHGGTA SGLPARSAPG GRTAPRHRRK GSAQLCSRPV PMGGKRCLQS
RLGALECSDR QVLRRKFPGL GSQQSGVLPP SPAVPALTGH ELSGRGHPPA EQSALQAPVS
LRPWEEAHRY SHASQSASDV PKANMEANVF KVVEKCPQHC YLLMNREGMN QRIKEWWLSW
LSEQCVHVGT GRLTVSKAAT EVILNVPETR VSPLENGLQV ASEDSGLSTC TVGLWIDAGS
RYENEKNNGT AHFLEHMAFK GTKKRSQLDL ELEIENMGAH LNAYTSREQT VYYAKAFSKD
LPRAVEILAD IIQNSTLGEA EIERERGVIL REMQEVETNL QEVVFDYLHA TAYQNTALGR
TILGPTENIK SINRNDLVEY ITTHYKGPRM VLAAAGGVSH DELLDLAKCH FGNLPSAPEG
GLPPLPPCSF TGSEIRIRDD KMPLAHLAIA VEAAGWADPD TIPLMVANTL IGNWDRSFGG
GVNLSSKLAQ TACHGNLCHS FQSFNTCYTD TGLWGLYMVC EPSTIEDMVH FVQREWIRLC
TSVTENEVAR AKNLLKTNML LQLDGSTPIC EDIGRQMLCY KRRIPIPELE ARIEAIDAQT
IREICTKYIC DKHPAVAAVG PIEQLPEYSK ICSGMN
//