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Database: UniProt
Entry: C5BS63_TERTT
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Original site: C5BS63_TERTT 
ID   C5BS63_TERTT            Unreviewed;       683 AA.
AC   C5BS63;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU003385};
GN   OrderedLocusNames=TERTU_3677 {ECO:0000313|EMBL:ACR14072.1};
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR14072.1, ECO:0000313|Proteomes:UP000009080};
RN   [1] {ECO:0000313|EMBL:ACR14072.1, ECO:0000313|Proteomes:UP000009080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(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}.
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DR   EMBL; CP001614; ACR14072.1; -; Genomic_DNA.
DR   RefSeq; WP_015820188.1; NC_012997.1.
DR   AlphaFoldDB; C5BS63; -.
DR   STRING; 377629.TERTU_3677; -.
DR   KEGG; ttu:TERTU_3677; -.
DR   eggNOG; COG1290; Bacteria.
DR   eggNOG; COG2857; Bacteria.
DR   HOGENOM; CLU_021957_0_0_6; -.
DR   OMA; LPWLDSA; -.
DR   OrthoDB; 9804503at2; -.
DR   Proteomes; UP000009080; 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; IPR009056; Cyt_c-like_dom.
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:SF37; CYTOCHROME B; 1.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF02167; Cytochrom_C1; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
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.
DR   PROSITE; PS51007; CYTC; 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:UP000009080};
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        86..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        149..167
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..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        351..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        382..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        420..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        656..674
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..411
FT                   /note="Cytochrome b/b6 C-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51003"
FT   DOMAIN          464..646
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         477
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT   BINDING         480
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT   BINDING         481
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
SQ   SEQUENCE   683 AA;  77351 MW;  E1F6ACA5827D0EB4 CRC64;
     MNNWLTGLWT WVDARLPVQR AWDTHMGKYY APKNFNFWYF FGVLSLLVLV NQLLTGIWLT
     MNYMPSAEEA FASVEYIMRD VPFGWIIRYM HSTGASAFFI VVYLHMFRGL MYGSYRKPRE
     LVWIFGMFIY VALMAEAFLG YVLPWGQMSY WGAQVIVNLF GAIPYVGEDL VQWIRGDYLI
     SGATLNRFFA LHVVAVPIVL LALVVLHILA LHEVGSNNPD GVEIKKNKDE NGIPLDGVPF
     HPYYSVHDLV GITVFLFVFC GVLFFAPEMN GFFLEHANFE QANSLKTPEH IAPVWYFTPF
     YAILRAVTFD LGGVFTSKFL GFVAMALAIV VLFFLPWLDR SPVKSIRYKG TISRVTLIIF
     AAAFVILGYL GLQAPTPART ALSQICTVIY FAYFIGLPFW SKMEKTLPEP ERLQAKGLPL
     PLVLAGLVFF LVLVFVPLKA VGSTGGACGE VPCDHFHADL NDKESLQRGA KYFVNYCMGC
     HSANYSRYER VAEDLDIPKD AMLNNMIFGD QKIGELMTIA MAPDKSKKWL GATPPDLTLV
     ARARSPEWVY TFLRNFYKDD SRPTGVNNKV FANVGMPHVL LELQGLQECA PGEHRDAHGH
     TVRNALGDPE LVACGSLKVG DVKGSMDKEE FDEAIHDLVN FMTYMSEPVA ESRVQIGIYV
     FMFLFVLLIF TWLLNREYWK DIH
//
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