(data stored in ACNUC7421 zone)

HOGENOM: CHLTB_1_PE109

ID   CHLTB_1_PE109                        STANDARD;      PRT;   431 AA.
AC   CHLTB_1_PE109; B0BAJ5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Na(+)-translocating NADH-quinone reductase subunit F;
DE   (CHLTB_1.PE109).
GN   Name=dmpP; OrderedLocusNames=CTLon_0109;
OS   CHLAMYDIA TRACHOMATIS L2B/UCH-1/PROCTITIS.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHLTB_1.PE109.
CC       Chlamydia trachomatis L2b/UCH-1/proctitis, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B0BAJ5_CHLTB
CC   -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to
CC       ubiquinol by two successive reactions, coupled with the transport
CC       of Na(+) ions from the cytoplasm to the periplasm. The first step
CC       is catalyzed by nqrF, which accepts electrons from NADH and
CC       reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer
CC       pathway (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + ubiquinone + Na(+)(In) = NAD(+) +
CC       ubiquinol + Na(+)(Out).
CC   -!- SUBUNIT: Composed of six subunits; nqrA, nqrB, nqrC, nqrD, nqrE
CC       and nqrF (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane (By similarity).
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -!- GENE_FAMILY: HOG000263661 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0BAJ5; -.
DR   EMBL; AM884177; CAP06507.1; -; Genomic_DNA.
DR   RefSeq; YP_001653212.1; NC_010280.1.
DR   ProteinModelPortal; B0BAJ5; -.
DR   STRING; B0BAJ5; -.
DR   GeneID; 5858885; -.
DR   GenomeReviews; AM884177_GR; CTLon_0109.
DR   KEGG; ctl:CTLon_0109; -.
DR   OMA; VQLECPP; -.
DR   ProtClustDB; PRK05464; -.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NADH or NADPH, quinone or similar compound as acceptor; IEA:InDR   GO; GO:0006814; P:sodium ion transport; IEA:HAMAP.
DR   GO; GO:0006814; P:sodium ion transport; IEA:HAMAP.
DR   HAMAP; MF_00430; NqrF; 1; -.
DR   InterPro; IPR012675; Beta-grasp_ferredoxin-type.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR010205; NADH_Q_Rdtase_suF.
DR   InterPro; IPR008333; OxRdtase_FAD-bd_dom.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   SUPFAM; SSF54292; Ferredoxin; 1.
DR   SUPFAM; SSF63380; Riboflavin_synthase_like_b-brl; 1.
DR   TIGRFAMs; TIGR01941; NqrF; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   HOGENOMDNA; CHLTB_1.PE109; -.
KW   2Fe-2S; Cell inner membrane; Cell membrane; Complete proteome; FAD;
KW   Flavoprotein; Ion transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; NAD; Oxidoreductase; Sodium; Sodium transport;
KW   Transport; Ubiquinone.
SQ   SEQUENCE   431 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTWLSGLYSI FVASAAFCSL DLILVAVILL SRKFLIKVHP CKLKINNDDS LTKTVDSGKT
     LLSSLLDSGI AIPSPCGGKA ACKQCKVRIT KNADEPLETD RSTFSKQQLE QGWRLSCQTK
     VQHDLCLEVE DRYFNASSWE GTVVSNENVA TFIKELVLSV DPSRPIPFKP GGYLQITVPP
     YKTNTSDWKQ TMDPQYYSDW ETFHLFDQVI DNLSLDTDSA NKAYSLASYP AELPLIKFNV
     RIATPSFVDQ APDPTIPWGV CSSYIFSLKP GDKVMVSGPY GESFMKENNR PVIFLIGGAG
     SSFGRSHILD LLLNKHSDRE LTLWYGARSL KENIYQEEYE KLEKEFPNFH YHLVLSQPLQ
     EDLDQGWDKN DPIKTNFLFK AFELGQLSHL PNPEDYLYYV CGPALHNSSI LTVLDNYGVE
     RSSIVLDDFG S
//

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