ID A0A9L9PXI7_HUMAN Unreviewed; 508 AA. AC A0A9L9PXI7; DT 13-SEP-2023, integrated into UniProtKB/TrEMBL. DT 13-SEP-2023, sequence version 1. DT 27-MAR-2024, entry version 4. 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:ENSP00000516392.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000516392.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000516392.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000516392.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-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}. 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; AC004668; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005250774.1; XM_005250717.3. DR SMR; A0A9L9PXI7; -. DR Ensembl; ENST00000706454.1; ENSP00000516392.1; ENSG00000105819.15. DR GeneID; 9512; -. DR HGNC; HGNC:9119; PMPCB. DR GeneTree; ENSGT00940000156608; -. DR Proteomes; UP000005640; Chromosome 7. DR GO; GO:0005739; C:mitochondrion; IEA:UniProt. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. 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 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:A0A9L9PXI7, KW ECO:0007829|MaxQB:A0A9L9PXI7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 68..214 FT /note="Peptidase M16 N-terminal" FT /evidence="ECO:0000259|Pfam:PF00675" FT DOMAIN 220..404 FT /note="Peptidase M16 C-terminal" FT /evidence="ECO:0000259|Pfam:PF05193" SQ SEQUENCE 508 AA; 56770 MW; D7E658877978DCB2 CRC64; MAAAAARVVL SSAARRRLWG FSESLLIRGA AGRSLYFGEN RLRSTQAATQ VVLNVPETRV TCLESGLRVA SEDSGLSTCT VGLWIDAGSR YENEKNNGTA HFLEHMAFKG TKKRSQLDLE LEIENMGAHL NAYTSREQTV YYAKAFSKDL PRAVEILADI IQNSTLGEAE IERERGVILR EMQEVETNLQ EVVFDYLHAT AYQNTALGRT ILGPTENIKS ISRKDLVDYI TTHYKGPRIV LAAAGGVSHD ELLDLAKFHF GDSLCTHKGE IPALPPCKFT GSEIRVRDDK MPLAHLAIAV EAVGWAHPDT ICLMVANTLI GNWDRSFGGG MNLSSKLAQL TCHGNLCHSF QSFNTSYTDT GLWGLYMVCE SSTVADMLHV VQKEWMRLCT SVTESEVARA RNLLKTNMLL QLDGSTPICE DIGRQMLCYN RRIPIPELEA RIDAVNAETI REVCTKYIYN RSPAIAAVGY NHRSELHEWK WNKLFSKRQT ISYSYVNILL PQPQPQYV //