ID F7XG09_SINMM Unreviewed; 327 AA.
AC F7XG09;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Cytochrome c oxidase chain II protein {ECO:0000313|EMBL:AEH83485.1};
GN OrderedLocusNames=SM11_pD0653 {ECO:0000313|EMBL:AEH83485.1};
OS Sinorhizobium meliloti (strain SM11).
OG Plasmid pSmeSM11d {ECO:0000313|EMBL:AEH83485.1,
OG ECO:0000313|Proteomes:UP000009045}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH83485.1, ECO:0000313|Proteomes:UP000009045};
RN [1] {ECO:0000313|EMBL:AEH83485.1, ECO:0000313|Proteomes:UP000009045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM11 {ECO:0000313|EMBL:AEH83485.1,
RC ECO:0000313|Proteomes:UP000009045};
RC PLASMID=pSmeSM11d {ECO:0000313|Proteomes:UP000009045};
RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT isolate SM11 extends the S. meliloti pan-genome.";
RL J. Biotechnol. 155:20-33(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00029368};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000256|ARBA:ARBA00007866}.
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DR EMBL; CP001832; AEH83485.1; -; Genomic_DNA.
DR RefSeq; WP_010975791.1; NZ_JAJJBH010000002.1.
DR AlphaFoldDB; F7XG09; -.
DR GeneID; 61600911; -.
DR KEGG; smx:SM11_pD0653; -.
DR PATRIC; fig|707241.3.peg.6342; -.
DR HOGENOM; CLU_036876_1_1_5; -.
DR Proteomes; UP000009045; Plasmid pSmeSM11d.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR CDD; cd04213; CuRO_CcO_Caa3_II; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034236; CuRO_CcO_Caa3_II.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1.
DR PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Plasmid {ECO:0000313|EMBL:AEH83485.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..225
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 235..327
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 327 AA; 35340 MW; BA022E4AA50FC73C CRC64;
MRLARYFAAA SALALQGCAG LQSALDPSGA EAERIGTLSW LLVLFSTAIL VAVCLITAVA
LFGGERWRAR IAGERIVIGG GLVFPILALS VLLIYGFYLM SPGTTEARSQ GALRIEVVGE
RWWWRVTYVD EAGRRIESAN EIRLPVGRPV ELELTSADVI HSFWVPRLAG KLDMIPGHTN
TLTLQATKAG ISRGQCAEYC GGPHAFMSFY VIAMPEDQFS SWLAGEAGDA SAAKPDQAAG
QALFLSSGCA ACHRVRGTDA RGTIGPDLTH VGSRHSLAAA TLENDVAAFV RWIRDGQHVK
PENLMPPFEI FTDDELRQLA AYLDQLR
//
