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Database: UniProt
Entry: D1B8X9_THEAS
LinkDB: D1B8X9_THEAS
Original site: D1B8X9_THEAS 
ID   D1B8X9_THEAS            Unreviewed;       903 AA.
AC   D1B8X9;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial {ECO:0000256|ARBA:ARBA00040751};
GN   OrderedLocusNames=Taci_0496 {ECO:0000313|EMBL:ACZ18732.1};
OS   Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS   (Selenomonas acidaminovorans).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC   Thermanaerovibrio.
OX   NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ18732.1, ECO:0000313|Proteomes:UP000002030};
RN   [1] {ECO:0000313|EMBL:ACZ18732.1, ECO:0000313|Proteomes:UP000002030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49978 / DSM 6589 / Su883
RC   {ECO:0000313|Proteomes:UP000002030};
RX   PubMed=21304665; DOI=10.4056/sigs.40645;
RA   Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA   Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA   Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT   "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT   (Su883).";
RL   Stand. Genomic Sci. 1:254-261(2009).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004443}; Matrix side
CC       {ECO:0000256|ARBA:ARBA00004443}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038146}.
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DR   EMBL; CP001818; ACZ18732.1; -; Genomic_DNA.
DR   RefSeq; WP_012869248.1; NC_013522.1.
DR   RefSeq; YP_003317014.1; NC_013522.1.
DR   AlphaFoldDB; D1B8X9; -.
DR   STRING; 525903.Taci_0496; -.
DR   EnsemblBacteria; ACZ18732; ACZ18732; Taci_0496.
DR   KEGG; tai:Taci_0496; -.
DR   PATRIC; fig|525903.6.peg.501; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_007487_1_1_0; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000002030; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
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:SF209; CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Hydrolase {ECO:0000313|EMBL:ACZ18732.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002030};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..903
FT                   /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003021340"
FT   DOMAIN          45..191
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          199..374
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          652..829
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   903 AA;  100390 MW;  A2216DDC2862D692 CRC64;
     MKHAIPLLVM GFLLVSWAPA FGAARVKAEP SIGGVTEYQL GNGLKVLLIR DPGASNVTVN
     VVYRVGSSDE RDGQRGLAHL LEHLLFKGTP SHPDIPSEIA ARGGRANGTT WTDRTCYFQT
     LPATMENLRW ALSLESERMT SARITAEELE RERGVVINEL VRGENDPVSV LLNRLSSVAF
     DWHTYGNSTI GNRRDLETVS LDEVLGFYRS FVRPDNGVLV IASPFEDREV LGEVEARFGS
     IPRPSHPVPR RVSQELGKDG DRFVRLRQPG QFRAVGALYH GPAGSSPEAA AFQVLMEVMG
     LEPSGGLYRE LVMKGLAGAV WAGSFLFRDS SMGLVLAQLP MDGNPDRAAE VMLSVLEDPS
     RIDQRDVEQA KQRLMKKMDL KYANPDDLAV ELTEWISRGD WRLFFAHRRR LEMVSVEDVR
     RVASRYLVRD NRTWGIFEPS DRRVLISTDG PRDVEPGELS ALGGLQEQGE AVGPSPEALE
     ARTSRFRVSG LKGAVINKRT RGGWVYGRLG LNFGNLSDLE GRSVIGEVLS RYLGRGAGDL
     SREEVQREFD RLRASVSFSG SATGVTVDLK VPVENLEGVL ALVARCLREP RFDEGELRVL
     KLEMRSEIED QLDDPSVLAE EELDRAFNPY PVGDVRRPVP MAERLRAIDS VRLRDLRDFH
     RRFFGLVDGE LAVVGPVEEG ALMGMMSSLF GGWVPRATYE RVPYPFVAVE GGRRRVEVPG
     KPNATVAAWA PLRLTQDSPD YPALLVAVNV LGGGWLDSRL ARRIRHQDGT SYGVRLSLNA
     FDPDESARLE FWAIAAPGDV ERVRESFYDE VRRALEGGFT AEEVSRAKAF ILEGVKVDRS
     QDGKLVRRME RDLYLGRDFG WHRRMEEAVG AVTSDSALEA LRRHLRGPEA FLLVEVGSFE
     GRP
//
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