ID A0A268S851_9BACL Unreviewed; 293 AA.
AC A0A268S851;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Menaquinol-cytochrome C reductase {ECO:0000313|EMBL:PAF28763.1};
GN ORFNames=CHI14_26355 {ECO:0000313|EMBL:PAF28763.1};
OS Paenibacillus sp. 7516.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2022549 {ECO:0000313|EMBL:PAF28763.1, ECO:0000313|Proteomes:UP000216732};
RN [1] {ECO:0000313|EMBL:PAF28763.1, ECO:0000313|Proteomes:UP000216732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7516 {ECO:0000313|EMBL:PAF28763.1,
RC ECO:0000313|Proteomes:UP000216732};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PAF28763.1}.
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DR EMBL; NPBI01000039; PAF28763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268S851; -.
DR Proteomes; UP000216732; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR PANTHER; PTHR37823; CYTOCHROME C-553-LIKE; 1.
DR PANTHER; PTHR37823:SF4; MENAQUINOL-CYTOCHROME C REDUCTASE CYTOCHROME B_C SUBUNIT; 1.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 210..290
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 173..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 293 AA; 32311 MW; BA839A8D7DAA76F3 CRC64;
MAHGHKPDDQ EKIIFVGDSR VRKGAGFITP PDYTAYPGKS EAFIPNFLLK EWMVGVVVLV
GILVLTISEP APLGYPANPS ASVIPMPDWY FLFLYQYLKY PYASGDYVLL GVLGVSGVAF
GALLLAPFLD TGKERRFYKR PIASSLMVLS ILSVFYLTNV AWTHYKHELE ATGQKPEHIQ
REEEAHEKHE QGLPTSNAPG QQQEVAIVDK DDPAMETLKK AGCISCHAAD LKGASGPSLR
GIGDKHSQEE ILTIIKEGYN GMPPMYDQAI AQGLTDDDIN HLAEWLAKQK AEQ
//
