ID C6PMK7_9CLOT Unreviewed; 495 AA.
AC C6PMK7;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Putative sensor with HAMP domain {ECO:0000313|EMBL:EET89471.1};
GN ORFNames=CcarbDRAFT_0060 {ECO:0000313|EMBL:EET89471.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET89471.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET89471.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET89471.1,
RC ECO:0000313|Proteomes:UP000004198};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT "The draft genome of Clostridium carboxidivorans P7.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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:EET89471.1}.
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DR EMBL; ACVI01000001; EET89471.1; -; Genomic_DNA.
DR AlphaFoldDB; C6PMK7; -.
DR STRING; 536227.Ccar_03010; -.
DR eggNOG; COG2972; Bacteria.
DR Proteomes; UP000004198; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000004198};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..256
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT COILED 70..97
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 261..288
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 495 AA; 57416 MW; 629F401486C94E7F CRC64;
MIVKSSSLRR KFIIFVLITI IPIATNSIIS FIISKQITYS YDSMLNKMSV TKEVKNSLND
SFTNFNKYMI ESSKESKEKY ETSYDKAMKN LILLEEKSDI HSKYILRDLQ NSLRSYKNSG
DAAIEISSKQ GGIDVYYDHY IFTKEIFSYS NTFLTQLSES YLSYNNEIYN KLKEKEKTIY
KVLLFYIITA LIISILYTLF FLKNILEKLR ELVDASKRVS YGDFSFYEGK KTFIYELDIL
SEAFSRMIHD IKKHINFIEE KAELEMKLRN EEMNLLKYQN ALKQSKLKVL QSQINPHFLF
NTLNCINQTA IRENALQTES LITSVSGILR YSLRMMDRNA SMEEEVTVVK QYMFIQQLRF
EDRIKFNLHV RGDLSKVLVP GMTLQPFVEN AFIHGIEPKE EGGVINIDIL EQGDVCTVLI
EDTGCGIDEK TLNKIISGDV GLEHTGHTTG MGIRSVVQRL ELIYGQKNIF RIESKKDFGT
KVYLKIPIKE LKDIC
//