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QOX2_STAS1
ID   QOX2_STAS1              Reviewed;         373 AA.
AC   Q49WI4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Probable quinol oxidase subunit 2;
DE            EC=1.10.3.-;
DE   AltName: Full=Quinol oxidase polypeptide II;
DE   Flags: Precursor;
GN   Name=qoxA; OrderedLocusNames=SSP1730;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC   -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC       oxygen to water. Subunit II transfers the electrons from a quinol to
CC       the binuclear center of the catalytic subunit I (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a quinol + O2 = 2 a quinone + 2 H2O; Xref=Rhea:RHEA:55376,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:132124;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AP008934; BAE18875.1; -; Genomic_DNA.
DR   RefSeq; WP_011303443.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49WI4; -.
DR   SMR; Q49WI4; -.
DR   STRING; 342451.SSP1730; -.
DR   EnsemblBacteria; BAE18875; BAE18875; SSP1730.
DR   KEGG; ssp:SSP1730; -.
DR   PATRIC; fig|342451.11.peg.1729; -.
DR   eggNOG; COG1622; Bacteria.
DR   HOGENOM; CLU_036876_6_0_9; -.
DR   OMA; TAMNSFF; -.
DR   OrthoDB; 1654242at2; -.
DR   Proteomes; UP000006371; 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:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR   CDD; cd04212; CuRO_UO_II; 1.
DR   Gene3D; 1.10.287.90; -; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR045187; CcO_II.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034227; CuRO_UO_II.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR   InterPro; IPR006332; QoxA.
DR   PANTHER; PTHR22888; PTHR22888; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   SUPFAM; SSF81464; SSF81464; 1.
DR   TIGRFAMs; TIGR01432; QOXA; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Lipoprotein; Membrane; Oxidoreductase;
KW   Palmitate; Reference proteome; Respiratory chain; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..373
FT                   /note="Probable quinol oxidase subunit 2"
FT                   /id="PRO_0000275883"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          292..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   373 AA;  42665 MW;  0519A00955824123 CRC64;
     MSKFKSLLLL FGSLILLSGC SNVEVLNPKG PMASDSKFLI MYSIIFMLVI IAAVLILFTV
     FLYKYRIGNT DESGKMHHNS LLETIWFIIP VIIVIALAIP TVNSLYNYEE KPQKEDDPLV
     VYATSAGYKW FFSYPEEKIE TVNHLTIPKD RPVVFKLQSM DMMTSFWIPQ LGGQKYAMTG
     MTMDWTLTAS EEGTFRGRNS NFNGEGFSRQ TFDVNSVSQS KFEDWVKDAK KQKVLDQDTF
     DKQLLPTTEN KNLTFSGTHL AFVDPAADPE YIFYAYDRYN FVQKDPNFNT EEERTADVLD
     KPDQPARKPE ITNANYERHG MKAMILGNNE PYDSEFKDEE SHNMDEMEKI SEGAKDEKAS
     KIEKKDHENG GGH
 
 
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