ID A0A0F4QPY0_9GAMM Unreviewed; 977 AA.
AC A0A0F4QPY0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TW85_23290 {ECO:0000313|EMBL:KJZ08687.1};
OS Marinomonas sp. S3726.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ08687.1, ECO:0000313|Proteomes:UP000033747};
RN [1] {ECO:0000313|EMBL:KJZ08687.1, ECO:0000313|Proteomes:UP000033747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3726 {ECO:0000313|EMBL:KJZ08687.1,
RC ECO:0000313|Proteomes:UP000033747};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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}.
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:KJZ08687.1}.
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DR EMBL; JXYC01000040; KJZ08687.1; -; Genomic_DNA.
DR RefSeq; WP_046019557.1; NZ_JXYC01000040.1.
DR AlphaFoldDB; A0A0F4QPY0; -.
DR PATRIC; fig|579484.3.peg.4779; -.
DR OrthoDB; 6110612at2; -.
DR Proteomes; UP000033747; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
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; 6.10.340.10; -; 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; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; 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 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; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF158472; HAMP domain-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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 1.
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 Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000033747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 174..227
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 232..278
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 390..608
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 636..754
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 795..887
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 338..376
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 685
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 836
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 977 AA; 109598 MW; A0C4F0217ECCAF77 CRC64;
MSFRLKTILG LILIQTTVFT ILYLVSMSVL QNSSEKAIQK RIYTVSNLFS AMAKDSVLSY
DLASLKTYVD EIIKHPDMVY VRVFDDHTNL LAAAKRENEQ IKPFIQDQNI QAVSDGIFDT
YTEIIEQETS YGRVEFGLDI NFARKDSAEA QNILVLISIL SIAVTVLFSF VLGKYLTRQL
TALAQGSKAL SKGDLSYRVK VSSGKDELTK TAQSFNEMAD KLNTLYFDVQ HEASFNRAIF
STSPSGIIIV DENGTIKQLN KAAEALFGNA EKQIINNNID TLIYSANKEN NYFLNSNIKE
NGNLMNEAEA IRQDNSRFPI YLAIGKMDVT EEAMYIVIVS DLTEKKRHEK ELDKYRKNLE
KTVKERTEEL IQARDSAEAG ARTKAAFLAN MSHEIRTPMN SIIGFTEMLL LKHSLPEKSR
KHLRTVLNSA QSLLVIINDI LDISKLESGK FVLEKTYFHL PNALALTLQT VDQQAKEKNL
DIKLEIDANL PHKYLGDPTR LRQVVLNLVS NSIKFTQEGH IRLYVKMDSK NKLHFIVQDT
GIGMSEIQVK SVFDSFVQAD ESTTRCFGGT GLGTTISKQI VNIMGGDIWV ESTLGEGSAF
HFTCILDVAD EELEQECLYE SDNMEVNEYN SPRKFKVLLT EDIDANAELV TIRLEHQGHT
VDWAKNGLEA VEATQKTNYD IILMDVMMPV MDGFEASREI RKNEIGSGQH IQILALTASV
MNEDYQNCLD SGMDAVEAKP INFNHLFSAM ENMVPSELGE INDTKDIEFY QQNNIDFSPL
REIANYTKAI EVWRSNDVYA KALKSFANER NSDALQIEQL LQQNKDDIQP AKAIAHALKG
LAGNLYLSQV AKIITEIDAD LKSNDSENAI LKLDSLMQAL DDACGAISQL NLSHLNQTNQ
PKPLDKEAMG PLLLELITAL NTLDPDVIEP LLDNLTQSIG HKKLHDIQRE VDAFNFEGAI
LKTQEVAINL GITLECD
//
