ID W2EX49_9ACTN Unreviewed; 544 AA.
AC W2EX49;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cytochrome bc1 complex cytochrome b subunit {ECO:0000256|ARBA:ARBA00016116};
DE EC=7.1.1.8 {ECO:0000256|ARBA:ARBA00012951};
DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrB {ECO:0000256|ARBA:ARBA00029568};
GN ORFNames=MPTA5024_09975 {ECO:0000313|EMBL:ETK36278.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK36278.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK36278.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK36278.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00029351};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETK36278.1}.
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DR EMBL; AWEV01000083; ETK36278.1; -; Genomic_DNA.
DR RefSeq; WP_036321693.1; NZ_KI866522.1.
DR AlphaFoldDB; W2EX49; -.
DR STRING; 316330.MPTA5024_09975; -.
DR PATRIC; fig|316330.3.peg.1934; -.
DR HOGENOM; CLU_031114_2_0_11; -.
DR OrthoDB; 9804503at2; -.
DR Proteomes; UP000018869; Unassembled WGS sequence.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR PANTHER; PTHR19271; CYTOCHROME B; 1.
DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR Pfam; PF13631; Cytochrom_B_N_2; 1.
DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018869};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..237
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT REGION 512..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 60257 MW; 82F3F12E403C8171 CRC64;
MDAPPKAIVG PSTFVDDRLG AGTFLKRNLR KIFPDHWSFL LGEIALYSFV ILLLTGTFLT
FWFKPSMGEV TYTGTYAPLY GVKMSEAYQS ALHISFDVRG GLLIRQIHHW AALLFVGGMM
AHALRIFFTG AYRKPREINW LIGIILLTLA LLEGLTGYSL PDDLLSGAGL RITEGVMLSI
PVIGTYLAFF LFGGEYPGHD VISRFYTIHI LLIPGILLAL ITAHMIIMWV QKHTQMAGKG
RTEHNVVGAP FYPAFMAKSG AFFLFTFAVI ALLGTFAQIN PIWLFGPYNP ANISAASQPD
WYMGFLEGAL RIMPSWEINL FDHTIPLSVL IPALVPLGLV MTGMALYPFI EQWVTGDRSE
HHIAERPRNN PHRTAIGISA ITFYGILWLL GANDVISANF KIDLYTTTWI GRFAIFIGPA
IAYFITYRMC IGLQRKDAEV LSHGVESGVI KRMPNGQYIE VHTPAAEDIA EHLRGKQEIP
VLTGAPDGEG IPPKSARTAL GRLRTRMSEA YGTDRVPLGN GHAHDEEHEE EHAAVGAGDR
KQLH
//
