位置:首页 > 蛋白库 > DHSC_BACSU
DHSC_BACSU
ID   DHSC_BACSU              Reviewed;         202 AA.
AC   P08064;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Succinate dehydrogenase cytochrome b558 subunit;
DE            Short=Cytochrome b-558;
GN   Name=sdhC; OrderedLocusNames=BSU28450;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / PY79;
RX   PubMed=3086287; DOI=10.1128/jb.166.3.1067-1071.1986;
RA   Magnusson K., Philips M.K., Guest J.R., Rutberg L.;
RT   "Nucleotide sequence of the gene for cytochrome b558 of the Bacillus
RT   subtilis succinate dehydrogenase complex.";
RL   J. Bacteriol. 166:1067-1071(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-202.
RC   STRAIN=168 / PY79;
RX   PubMed=3027051; DOI=10.1128/jb.169.2.864-873.1987;
RA   Phillips M.K., Hederstedt L., Hasnain S., Rutberg L., Guest J.R.;
RT   "Nucleotide sequence encoding the flavoprotein and iron-sulfur protein
RT   subunits of the Bacillus subtilis PY79 succinate dehydrogenase complex.";
RL   J. Bacteriol. 169:864-873(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX   PubMed=3036777; DOI=10.1128/jb.169.7.3232-3236.1987;
RA   Melin L., Magnusson K., Rutberg L.;
RT   "Identification of the promoter of the Bacillus subtilis sdh operon.";
RL   J. Bacteriol. 169:3232-3236(1987).
RN   [6]
RP   TOPOLOGY, AND HEME-BINDING.
RX   PubMed=2120540; DOI=10.1111/j.1365-2958.1990.tb00677.x;
RA   Friden H., Hederstedt L.;
RT   "Role of His residues in Bacillus subtilis cytochrome b558 for haem binding
RT   and assembly of succinate: quinone oxidoreductase (complex II).";
RL   Mol. Microbiol. 4:1045-1056(1990).
CC   -!- FUNCTION: Di-heme cytochrome of the succinate dehydrogenase complex.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is +65 mV.;
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Part of an enzyme complex containing three subunits: a
CC       flavoprotein, an iron-sulfur protein and cytochrome b-558.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome b558 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M13470; AAA22745.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99546.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14805.1; -; Genomic_DNA.
DR   EMBL; M16753; AAA22749.1; -; Genomic_DNA.
DR   PIR; A29843; DEBSSC.
DR   RefSeq; NP_390723.1; NC_000964.3.
DR   RefSeq; WP_003222512.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P08064; -.
DR   SMR; P08064; -.
DR   STRING; 224308.BSU28450; -.
DR   PaxDb; P08064; -.
DR   PRIDE; P08064; -.
DR   EnsemblBacteria; CAB14805; CAB14805; BSU_28450.
DR   GeneID; 64304571; -.
DR   GeneID; 937458; -.
DR   KEGG; bsu:BSU28450; -.
DR   PATRIC; fig|224308.179.peg.3090; -.
DR   eggNOG; COG2009; Bacteria.
DR   InParanoid; P08064; -.
DR   OMA; YDMMANI; -.
DR   PhylomeDB; P08064; -.
DR   BioCyc; BSUB:BSU28450-MON; -.
DR   BioCyc; MetaCyc:BSU28450-MON; -.
DR   UniPathway; UPA00223; -.
DR   PRO; PR:P08064; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd03497; SQR_TypeB_1_TM; 1.
DR   Gene3D; 1.20.1300.10; -; 1.
DR   InterPro; IPR011138; Cytochrome_b-558.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR016002; Succ_DH_cyt_b558_Firmicute.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   PIRSF; PIRSF000170; Succ_dh_cyt_b558; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
DR   TIGRFAMs; TIGR02046; sdhC_b558_fam; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..202
FT                   /note="Succinate dehydrogenase cytochrome b558 subunit"
FT                   /id="PRO_0000199876"
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         28
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305"
FT   BINDING         70
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305"
FT   BINDING         113
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255"
FT   BINDING         155
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  22931 MW;  831352DD07570DD3 CRC64;
     MSGNREFYFR RLHSLLGVIP VGIFLIQHLV VNQFAARGAE AFNSAAHFMD SLPFRYALEI
     FIIFLPLIYH AVYGVYIAFT AKNNAGQYSY MRNWLFVLQR VTGIITLIFV SWHVWETRIA
     AQMGAEVNFD MMANILSSPA MLGFYIVGVL STIFHFSNGL WSFAVTWGIT VTPRSQRIST
     YVTLIIFVAL SYVGLKAIFA FV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024