ID Q8EAA6_SHEON Unreviewed; 1702 AA.
AC Q8EAA6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=SO_4002 {ECO:0000313|EMBL:AAN56976.2};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN56976.2, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN56976.2, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN56976.2,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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}. Periplasm
CC {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000256|ARBA:ARBA00007639}.
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DR EMBL; AE014299; AAN56976.2; -; Genomic_DNA.
DR RefSeq; NP_719532.2; NC_004347.2.
DR STRING; 211586.SO_4002; -.
DR PaxDb; 211586-SO_4002; -.
DR KEGG; son:SO_4002; -.
DR PATRIC; fig|211586.12.peg.3881; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG1879; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_002937_0_0_6; -.
DR OrthoDB; 9810730at2; -.
DR PhylomeDB; Q8EAA6; -.
DR BioCyc; SONE211586:G1GMP-3706-MONOMER; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
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; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF13188; PAS_8; 2.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00062; PBPb; 1.
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; SSF53822; Periplasmic binding protein-like I; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Kinase {ECO:0000313|EMBL:AAN56976.2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008186};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:AAN56976.2};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00023065};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 975..1196
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1351..1467
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1511..1613
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1400
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1550
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1702 AA; 188107 MW; 2CE3F7FC4A684808 CRC64;
MVKGARLSQL GVIMAGYGLI SLAILMILSA FKLVNMRTRY LAQLPLQSNV LWRLFPILFA
FLFSSLSVLA SPGGQIPLTT AVIDRVSAPT PVLRVSMILS VDTPFNRQIG ARAQAAAVDL
NIQLQVLYAD GTHDGLMTLG REVMNQGIDG LIFSPVDDFG EALIREAQKL KIPVVTLRAK
LDMLSSAALA ELPNFIANVN INDQKSGQLL MHYLLSVDQL NRDVPAVLLI AGPQGYPNVE
RGVEDVQRFM NSLSTRGTLK IAYTDWSVEQ ALAQFDSAIA AQPALTTVVT MNASAAVAVA
AKAHQQLGAN APAIGSMIWS ESLVQDIKQG KIQAAITGSE FSGAIALSIL FDHLSARGGP
SRKGSFVAPL VVITPNNYQD YESILDFDPL RLNFRQISQH FNPDLSINEL RLADLLTSEA
RVNFLKTLTE PELNFLRQHP SIRVGIEPDG APIDYVDQAG KHTGLIASYL SEIAKLIPVR
FEVQPTQSWG QTLKDFAADK LDMISLISAS EDRKQRILFT DAIGHFPAVI VMRKDAELVD
GIEGLFGKTV AVTRGDITEE LLRKKYPEIN IIAFDRLEDV LSTTLASQVD AAVMLLPKAG
QSLLSPANKE LTIVAPLDDE FEHSIGVRRD WPELQSILNK ALAQIPSSTR AELDSRWFTV
KYDFGMDPQQ IKRWAISSAM VILGLFACFI LWNYGLKREL LRRSRMAAQL ESSMNKFHAL
FDSVMDACVI IDKRGVIKEC NAALQTLLGV EDKTALVGTS LTQFHLADTF MGSAVQIAQS
VEDVLKQGLL KFEADITDSQ GQSIPAEVTL KSIELNTERF VLATYHNLAE RRLVDRLIRH
ERNLLKNVLG MSPIGVWVCV NGTCRYVNAQ MTLMTGLEVE HAVADIFLQP KDYWHYIREL
APEQECITFE SKLKGYHGQI LDVLFTAYPT FYDGQHANLC WALDITQEKA IQAELASAKL
QADAANRAKS DFLANMSHEI RTPMNAIIGM SYLALQTDLA EKRKDYIAKV HQAAGSLLNI
INDILDFSKI EANKLTVEHI EFDLDEVLTQ LNNVIGFKVE ENSMRLIYDI ATDCPRYFIG
DPQRLGQILL NYCNNAVKFS PKGSDILLSC QAELDKQGAT LTFCVADDGI GIPLDKQARL
FHSFEQGDTS TSRKYGGTGL GLAICKRLSE LMQGEVWCES ELGQGSRFYL RLHLPLVKPY
DLSTQFAALQ GESLSIVGFM PDLSAIYSRF AARVGMQART LEMHMALAEL SACTSQHLIM
CETNAFEPEL LSVVLANDKL GLLLIGNGSE PVAIQSLVDK HPQIIAKQHP ILLRTLGESL
LLLLNRDRAP FGQHLEHQSI TTLKNQLAGV ELLLVEDNYL NQELAVELLR QAGARVTVAQ
HGQEALTLLA QQSFDCVLMD GQMPVMDGYE ATRLIRAQPQ FADLPIIAMT ANAMDSDRER
ALAAGMNAQI NKPFQVQQLY STIAQHVSVH SVQSLPESPE AHDLDKAQLK QGLPLVEELD
IDAGLALCNY NADLYRHLLT LFVQTGAKLL QNQQNEFSQD NLSALRLSLH TLKGVAGNIG
AVSLKEDSGR LEASLTDISS LQQLDANIQE TVSQEIHLLH AKLQQLLTLL AEWQTVNQPD
EASQSISMTE LMRLFAQLTQ NLKEYNTDAL SLVERLSQLT VLQPQRQLIA ELKQATGQFD
FSQGLELAIQ LQEWAQQQLA KE
//
