ID I4W1L1_9GAMM Unreviewed; 481 AA.
AC I4W1L1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UU7_09345 {ECO:0000313|EMBL:EIL93352.1};
OS Rhodanobacter spathiphylli B39.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL93352.1, ECO:0000313|Proteomes:UP000003226};
RN [1] {ECO:0000313|EMBL:EIL93352.1, ECO:0000313|Proteomes:UP000003226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B39 {ECO:0000313|EMBL:EIL93352.1,
RC ECO:0000313|Proteomes:UP000003226};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(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};
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:EIL93352.1}.
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DR EMBL; AJXT01000021; EIL93352.1; -; Genomic_DNA.
DR RefSeq; WP_007807655.1; NZ_AJXT01000021.1.
DR AlphaFoldDB; I4W1L1; -.
DR STRING; 1163407.UU7_09345; -.
DR PATRIC; fig|1163407.3.peg.1883; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000003226; Unassembled WGS sequence.
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 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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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:EIL93352.1};
KW Ion transport {ECO:0000313|EMBL:EIL93352.1};
KW Kinase {ECO:0000313|EMBL:EIL93352.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003226};
KW Transferase {ECO:0000313|EMBL:EIL93352.1};
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:EIL93352.1}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..475
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 481 AA; 51551 MW; 9ACEA209C8589458 CRC64;
MHEPASRRRR GSVVADYLFA TMVTLAAFAL TFVADRYLSI ANLSLILLTA VLAVAVRKRM
AVAVYTAVLC FIGDNFFFTR PRHTLAVASA DDVLAIGLFL IVALVCSRMA TRLSSQVGSL
RAAQLRARTL LQLGKQLAAA ADAAGIRQVG SQALTQAIGA TARMQLAAGD PAAKVASVDP
GADLDGEWVI PLIVGTHDHG AVVFAAHEPG EPDAERRELA VAMGQDIALA LERARLADEL
EQARVQGETE RLRNALLSSV SHDLRSPLAC MIGAADTLAM YETQLPQGER QELLQAILHE
GQRLDRYIQN LLDMTRLGHG TLKLHRDWVD VTEVVVAATD RLHRLFPEQP VQTGLPPDTV
LLYVHPALIE QALFNVLENA AHFSPPGEAV RIEAGAMGEQ LRIDVIDRGP GIPPDERARI
FDMFYSVSRG DRGNKGTGLG LSICRGMIGA HGGSVEALPT AGGGTTIRII LPLPPAPETS
T
//
