ID H8Z213_9GAMM Unreviewed; 1319 AA.
AC H8Z213;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Thi970DRAFT_01750 {ECO:0000313|EMBL:EIC21538.1};
OS Thiorhodovibrio frisius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodovibrio.
OX NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC21538.1, ECO:0000313|Proteomes:UP000002964};
RN [1] {ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIC21538.1, ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|EMBL:EIC21538.1,
RC ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Overmann J., Frigaard N.-U., Bryant D., Woyke T.;
RL Submitted (NOV-2011) 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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JH603169; EIC21538.1; -; Genomic_DNA.
DR RefSeq; WP_009148123.1; NZ_JH603169.1.
DR STRING; 631362.Thi970DRAFT_01750; -.
DR eggNOG; COG0715; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_86_3_6; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000002964; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015168; SsuA/THI5.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF09084; NMT1; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002964};
KW Signal {ECO:0000256|SAM:SignalP};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1319
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003618051"
FT DOMAIN 376..446
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 455..507
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 508..552
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 571..629
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 668..898
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 922..1042
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1104..1206
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 620..647
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 971
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1143
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1319 AA; 144994 MW; 89A16BFDE569676B CRC64;
MKITSCRMRQ HGLLAGLLAA LLLHAAPGIA LEPVRVQLKW THAFQFAGYY AAQSQGYYRD
AGLEVELVEA RPDTDVVAEV VSGRAQFGIG TSSLLLARAA GQPVVALATI FQHSPLVLLA
RRDNDLQSIH DLAGKPVMIE RQAEELLAYL AAEDVPLDTI DIIEHQFDFR DLIEGRAQAI
SAYSTNEVFF LQQAELPFSI FSPRSAGIDF YGDNLFTSEA ELDRHPSRVA AFLDASLRGW
AYALAHPQEV IDDILARDIS DPPPSRAFLT FEAEQTAKLI RADLVEIGYM NPGRWQHIAA
VYADLGMLER DFPVADMLYG APERGALPAW LRLSMGGALV LILLSFAITW QFRRINRRLR
ASLAESARIR HELSQSEEKF RHLTEHSSDI IWHLDSDLRF TYISLADERL RGFPREEVLG
QTVWSLLKPE GIEQIQQANA QRLERESQAK STSTQCYELE QKCKNGGWLW TEINVAPMRD
DQGQISGYYG VTRDISARRA AELALRASER RYRLLFERSP AGVFLFDQDL QLLDCNQRLA
TILQTSRERL IGLDLSKLRD RGLIPALQAA LTGEEGLFEG LYRATISEAE VWLSGRVAPL
YDDAGRISGG IAVFEDVGER KRAEAVIEAS RQELERANRA LRASSQEAMT MAERAEAANR
AKSQFLANMS HEIRTPMNAV LGMTHLTLRT ELTDHQRNYL NEIQTAAQSL LLIIDDILDF
SKIEANKLVL EHAPFHLRSA LAQVERLLCV KAQEKGVALR LELAPDLPNQ VQGDRLRLGQ
VLINLINNAI KFTTQGQVVL RVAPAAGPKE HEATPEQPEA ITLDFEVRDT GVGMSEEQMA
RLFEPFAQGD SSITRRYGGT GLGLAISREL VERMGGTLWV RSELGQGSTF GFALAFERVA
DSATHHEPVP AEAPALDLHG RRLLVVDDNR VNRVLIEELL RPFGASIATA DSGEAAVARV
TAEPFDLVLM DIQMPGMDGL TATRRIRAWE ERQADQSHLP IIAMTAHALR GDEAKSLAAG
MDAHLTKPID LDKLVATLAR WLRAELASAG ATDWPVERAT GQPTGWPMTR EAGHASADNS
AGPPPLRDCP PFEIAAALHR CNDDLALLVK LIDTFVAEFA DLVPELRAHL QDGHWAQARL
RAHSLKGSAA TLALESLARA ARELEAAIEA TAESLPESSN TQPLESNLPA SLASALAHLE
TLLPAALSAA RQLLGEVRIP AAAPDPASDV AKLSQTDLDE ALQHLRDKLD INAVDARLDF
QNLRQSLEAR ISSPDIEALA AALARLDFPN ASKHLGSIVD ILRTDSAAVS AQAPAPTPT
//
