ID A4A5E3_9GAMM Unreviewed; 676 AA.
AC A4A5E3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU003385};
GN ORFNames=KT71_10312 {ECO:0000313|EMBL:EAQ99014.1};
OS Congregibacter litoralis KT71.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Congregibacter.
OX NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ99014.1, ECO:0000313|Proteomes:UP000019205};
RN [1] {ECO:0000313|EMBL:EAQ99014.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ99014.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT "Characterization of a marine gammaproteobacterium capable of aerobic
RT anoxygenic photosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN [2] {ECO:0000313|EMBL:EAQ99014.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ99014.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT "The photosynthetic apparatus and its regulation in the aerobic
RT gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL PLoS ONE 4:E4866-E4866(2009).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC that generates an electrochemical potential coupled to ATP synthesis.
CC {ECO:0000256|RuleBase:RU003385}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|RuleBase:RU003385};
CC Note=Binds 2 heme groups non-covalently.
CC {ECO:0000256|RuleBase:RU003385};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR602326-1};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR602326-1};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000256|ARBA:ARBA00011649,
CC ECO:0000256|RuleBase:RU003385}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome b family.
CC {ECO:0000256|RuleBase:RU003385}.
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:EAQ99014.1}.
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DR EMBL; AAOA02000003; EAQ99014.1; -; Genomic_DNA.
DR RefSeq; WP_008294496.1; NZ_CM002299.1.
DR AlphaFoldDB; A4A5E3; -.
DR STRING; 314285.KT71_10312; -.
DR eggNOG; COG1290; Bacteria.
DR eggNOG; COG2857; Bacteria.
DR HOGENOM; CLU_021957_0_0_6; -.
DR OrthoDB; 9804503at2; -.
DR Proteomes; UP000019205; Chromosome.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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 GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR CDD; cd00284; Cytochrome_b_N; 1.
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; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR048259; Cytochrome_b_N_euk/bac.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR PANTHER; PTHR19271; CYTOCHROME B; 1.
DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU003385};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602326-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602326-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602326-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019205};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU003385};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003385};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003385}.
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..220
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT DOMAIN 230..403
FT /note="Cytochrome b/b6 C-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51003"
FT BINDING 471
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 474
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 475
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
SQ SEQUENCE 676 AA; 75933 MW; 523E2FC09B5A127C CRC64;
MVNMLIGLRD WVDERLPITR AWNTHMGEYY APKNFNFWYY FGVFSLLVLV NQLLTGVWLT
MNYTPSAEEA FASVEYIMRD VDYGWVLRYM HSTGASAFFI VVYLHMFRAM IYGSYKKPRE
LLWVFGMLIF VLLMAEAFVG YVLPWGQMSY WGAQVIISLF GAIPVVGESI VTWIRGDYLI
SGITLNRFFA LHVVALPIVL LALVVLHILA LHEVGSNNPD GIEIKKNKGP DGVPLDGIRF
HPYYSVHDVQ AIAVFLFVFC AIMFFAPEMG GFFLEYANFE EANALKTPDH IAPVWYFTPF
YSVLRAVPDK FWGFVAFAAS VAIPFVLPWL DRSPVKSWRY RGNLNKVMLV LFVASFLILG
VLGVKSPTPA RTALAQICSI FYFAFFLLMP IWSSMDKAKP VPERVTMDGG VGAVGSLAGL
LLILALTIIP LKVVGAESAY NCGTMPCDEV EMDISNKSSL QNGAKVYMNY CMGCHSLQYA
RYNRVADDLG IPEDLMRGNI IADPEVKVGA LMENAMDSDR AKVWFGAAPP DLTLVARARN
PEWLYTYLRT FYADPTRPYG VNNRVFPNVG MPHALIELQG LLACTPTAVH GEVEPLSGTQ
MADHSDPCGT MDVVDAGLMS TEEFDEATYD LVNFLAYVAE PIKADRQRIG IYSLLFLAVF
FVFATLLNRE YWKDVH
//
