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Database: UniProt
Entry: A0A0J1BRP0_9MICC
LinkDB: A0A0J1BRP0_9MICC
Original site: A0A0J1BRP0_9MICC 
ID   A0A0J1BRP0_9MICC        Unreviewed;       131 AA.
AC   A0A0J1BRP0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:KLU09122.1};
GN   ORFNames=ABL57_13615 {ECO:0000313|EMBL:KLU09122.1};
OS   Kocuria sp. SM24M-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1660349 {ECO:0000313|EMBL:KLU09122.1, ECO:0000313|Proteomes:UP000036489};
RN   [1] {ECO:0000313|EMBL:KLU09122.1, ECO:0000313|Proteomes:UP000036489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM24M-10 {ECO:0000313|EMBL:KLU09122.1,
RC   ECO:0000313|Proteomes:UP000036489};
RA   Palermo B.R., Castro D.B., Cauz A.C., Magalhaes B.L., Carlos C.,
RA   Costa F.L., Scagion G.P., Higac J.H., Pereira L.B., Almeida L.D.,
RA   Neves M.S., Cordeiro M.A., Prado P.F., Silva T.M., Balsalobre T.W.,
RA   Paulino L.C., Vicentini R., Ferraz L.F., Ottoboni L.M.;
RT   "Draft genome sequence of Kocuria sp. SM24M-10 isolated from coral mucus.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SIMILARITY: Belongs to the cytochrome b560 family.
CC       {ECO:0000256|ARBA:ARBA00007244}.
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:KLU09122.1}.
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DR   EMBL; LDNX01000120; KLU09122.1; -; Genomic_DNA.
DR   RefSeq; WP_047804024.1; NZ_LDNX01000120.1.
DR   AlphaFoldDB; A0A0J1BRP0; -.
DR   PATRIC; fig|1660349.3.peg.698; -.
DR   OrthoDB; 276905at2; -.
DR   Proteomes; UP000036489; Unassembled WGS sequence.
DR   GO; GO:0045281; C:succinate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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:InterPro.
DR   CDD; cd03501; SQR_TypeA_SdhC_like; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   InterPro; IPR039023; SdhC_prok.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR014314; Succ_DH_cytb556.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   NCBIfam; TIGR02970; succ_dehyd_cytB; 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   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   131 AA;  14760 MW;  C7F74D4CC8CE5835 CRC64;
     MAKTSKGTLY RGQAHGQWSW VAHRITGVAI FFFLLVHVLD TALVRVSPEA YNAVMETYKN
     PVMGLGEAGL VAAIVYHAFN GLRIILVDFW SQGTRYQKQM LWGVLVLWLV VMVPFLVRHL
     SNIFHLSIFG G
//
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