ID E6W7A9_DESIS Unreviewed; 582 AA.
AC E6W7A9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Selin_1543 {ECO:0000313|EMBL:ADU66276.1};
OS Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC Desulfurispirillum.
OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU66276.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU66276.1, ECO:0000313|Proteomes:UP000002572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC {ECO:0000313|Proteomes:UP000002572};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA Bini E., Woyke T.;
RT "Complete sequence of Desulfurispirillum indicum S5.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP002432; ADU66276.1; -; Genomic_DNA.
DR RefSeq; WP_013506157.1; NC_014836.1.
DR AlphaFoldDB; E6W7A9; -.
DR STRING; 653733.Selin_1543; -.
DR KEGG; din:Selin_1543; -.
DR eggNOG; COG3275; Bacteria.
DR HOGENOM; CLU_020473_3_3_0; -.
DR InParanoid; E6W7A9; -.
DR OrthoDB; 2514702at2; -.
DR Proteomes; UP000002572; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ADU66276.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572};
KW Transferase {ECO:0000313|EMBL:ADU66276.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 458..568
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 582 AA; 65316 MW; CC06F0F4956132E0 CRC64;
MFFSLVLDVD IKSNFHLFIQ LFQQIGVYGI IILLLGKHTW VRHCFYDRTD IKCQARLLVF
FLLIITVGEF LATAYHGTRL YSTSAVVIAA GYLLGSMFWG LVLGAIAGLY HFILGDWAGA
AQFTASAIIG FLAGYFGRNA FRFNLKLIPI VFFLAFLKVL IFYVMLSDYP VALFLLIKSG
VATFASDFFG GLLLLFMLNF MNSEQEKEHS FATSNALQIA SKTIVFFKGG FTADGARQVC
SIIHRSIPVD VVAITDHEQV LSAYGTIDDE VHGDGARLFD RDARKAIRTG EIVYSKRERR
RKGNRLPYHG LYVPLKASDE VTGLLVLRNW GSRSFSPYVM ELISGLQQLI GVQIEFAKLQ
KHKELSIQAE LLALQRQINP HFFFNSLNTI MSLIRIDPPK ARRLLLKMSE IFRVTFKSTA
ETVPLSTELE IVQGYLELEK ARFGDNISVQ LDISPPAMKY HLPQLIVQPL VENSFAHGFK
GRTGKWLIDI KAHYEEGRFS LKICDNGHGV AREQLRNIMQ MGVGKGSGVG LSNVYERLRN
LYGSRLAFAV DSDTGKGFTI TIVITDAQEK ESRNQAGVFG DH
//
