GenomeNet

Database: UniProt
Entry: G5JG14_9STAP
LinkDB: G5JG14_9STAP
Original site: G5JG14_9STAP 
ID   G5JG14_9STAP            Unreviewed;       204 AA.
AC   G5JG14;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Succinate dehydrogenase, cytochrome b558 subunit {ECO:0000313|EMBL:EHJ08869.1};
GN   ORFNames=SS7213T_01893 {ECO:0000313|EMBL:EHJ08869.1};
OS   Staphylococcus simiae CCM 7213 = CCUG 51256.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=911238 {ECO:0000313|EMBL:EHJ08869.1, ECO:0000313|Proteomes:UP000005413};
RN   [1] {ECO:0000313|EMBL:EHJ08869.1, ECO:0000313|Proteomes:UP000005413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 7213 {ECO:0000313|EMBL:EHJ08869.1,
RC   ECO:0000313|Proteomes:UP000005413};
RX   PubMed=22272658; DOI=10.1186/1471-2164-13-38;
RA   Suzuki H., Lefebure T., Pavinski Bitar P., Stanhope M.J.;
RT   "Comparative genomic analysis of the genus Staphylococcus including
RT   Staphylococcus aureus and its newly described sister species Staphylococcus
RT   simiae.";
RL   BMC Genomics 13:38-38(2012).
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:EHJ08869.1}.
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; AEUN01000036; EHJ08869.1; -; Genomic_DNA.
DR   RefSeq; WP_002462024.1; NZ_AEUN01000036.1.
DR   AlphaFoldDB; G5JG14; -.
DR   PATRIC; fig|911238.3.peg.350; -.
DR   OrthoDB; 9789209at2; -.
DR   Proteomes; UP000005413; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   CDD; cd03497; SQR_TypeB_1_TM; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   InterPro; IPR011138; Cytochrome_b-558.
DR   InterPro; IPR039023; SdhC_prok.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR016002; Succ_DH_cyt_b558_Firmicute.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   NCBIfam; TIGR02046; sdhC_b558_fam; 1.
DR   PANTHER; PTHR41910; SUCCINATE DEHYDROGENASE 2 MEMBRANE SUBUNIT SDHC; 1.
DR   PANTHER; PTHR41910:SF1; SUCCINATE DEHYDROGENASE 2 MEMBRANE SUBUNIT SDHC; 1.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   PIRSF; PIRSF000170; Succ_dh_cyt_b558; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000170-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000170-1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000170-1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        180..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         29
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:0000256|PIRSR:PIRSR000170-1"
FT   BINDING         71
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:0000256|PIRSR:PIRSR000170-1"
FT   BINDING         114
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:0000256|PIRSR:PIRSR000170-1"
FT   BINDING         157
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:0000256|PIRSR:PIRSR000170-1"
SQ   SEQUENCE   204 AA;  23569 MW;  37BF5B8E4F8AC158 CRC64;
     MAQTKNEYYL RRIHSLLGII PIGAFLVVHL LVNHQATQGA EAFNKASSFM ESLPFLIVVE
     FLFIYIPLLY HGLFGLHIAF TAKENVGHYS LFRNWMFLFQ RISGILAFIF IGVHLWQTRL
     QKAFFGKEVD YDMMHQTLQN PVWAIIYIIC IIAVVFHFSN GLWSFLVTWG VLQSPKSQRV
     FTWVSLIVFL VISYIGVTAI IAFM
//
DBGET integrated database retrieval system