ID I4D558_DESAJ Unreviewed; 891 AA.
AC I4D558;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Desaci_1955 {ECO:0000313|EMBL:AFM40932.1};
OS Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM40932.1, ECO:0000313|Proteomes:UP000002892};
RN [1] {ECO:0000313|EMBL:AFM40932.1, ECO:0000313|Proteomes:UP000002892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22704 / JCM 16185 / SJ4
RC {ECO:0000313|Proteomes:UP000002892};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
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};
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DR EMBL; CP003639; AFM40932.1; -; Genomic_DNA.
DR RefSeq; WP_014826938.1; NC_018068.1.
DR AlphaFoldDB; I4D558; -.
DR STRING; 646529.Desaci_1955; -.
DR KEGG; dai:Desaci_1955; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_0_9; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000002892; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion channel {ECO:0000313|EMBL:AFM40932.1};
KW Ion transport {ECO:0000313|EMBL:AFM40932.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFM40932.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000313|EMBL:AFM40932.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 392..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 663..879
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 891 AA; 98866 MW; 4AFAD7D4380DAEB1 CRC64;
MKNQGKLTVF LGAVAGVGKT YAMLEAAKER LSEGTDVVIG FVETHGSLET ETVLKGIPYI
SSKTQEFLGK LVQEMDLEVL LERHPQLVVV DELAHTNIPG SRHRKRYQDV EELLASGIDV
YTTLNIQHLE SLNDVVAQIT GVTVSETVPD RILEIASQIQ MVDITPDELI QRLKEGKVNV
PGVAAEAIEK FFRPGNINAL REMSLRYTAK RVDCQMESYM RNHGIAGPWP SGEKVMVCVS
GNPFSTKLIR TAKRMAARQN AEWLAVHVVL PGEMQKNENE KDLMEENLRM AEKLGAEIVT
PHGDDIVEEL LTLARKRNVS QIIIGKPERA RFQELFHGSV VDKVIRRSHG ISVHVISGRK
NAADRKRETI AEDNNTSLGH LSRRQRYSAT PYLMSVLMMS ALTVAVSPIE TFLGPVNIPM
LYLLPVLLTA ARWGRLPALI TAGMGVIIFD YFFVPPFYTL HVDDFRYVIS FVILMIAGIV
TGTLSGRLTD QINYSRQREQ QVSALYSLSR DLTAVDKLER ILDSIARKIG ETLDGQVVLL
LPDERNNLVL SQSSSTDHFM TESEMNVASW VYERGQKAGR GTETLRSAKA LYLPLITEQG
THGVLGICFF HQNDIVSPQQ IRFLDAFAGL AALAINRIKL ADEARQAHAL AESERLRTAL
FNSLSHDLRT PLSSIIGAAT GLLEDEDVVY SPDARHDLLQ TILQGAERMN RFVNNLLDMA
RLESGMLKLH KDWCDIQDII GVAINRLDIV LAKRLLDINI PAGLPLVQAD YALIEQVIVN
LLDNAVKYSE PVSKIVISVK QVGQNLEISV ANRGNPIPET DLSKVFDKFY RLTSPLQVSG
SGLGLSICKG IIESHNGDIW AENNELGGVT IIFTLPLEYE LSDKLPIEGG D
//
