ID A6VU89_MARMS Unreviewed; 1121 AA.
AC A6VU89;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mmwyl1_1087 {ECO:0000313|EMBL:ABR70018.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR70018.1};
RN [1] {ECO:0000313|EMBL:ABR70018.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR70018.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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; CP000749; ABR70018.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VU89; -.
DR STRING; 400668.Mmwyl1_1087; -.
DR KEGG; mmw:Mmwyl1_1087; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3300; Bacteria.
DR HOGENOM; CLU_000445_114_35_6; -.
DR OrthoDB; 6110612at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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 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; IPR005330; MHYT_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
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; 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; PF03707; MHYT; 3.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
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; 2.
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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50924; MHYT; 1.
DR PROSITE; PS50113; PAC; 1.
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 Kinase {ECO:0000313|EMBL:ABR70018.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00244};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ABR70018.1};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 24..47
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 59..83
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 121..145
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 157..180
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 192..218
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT DOMAIN 22..218
FT /note="MHYT"
FT /evidence="ECO:0000259|PROSITE:PS50924"
FT DOMAIN 270..315
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 399..473
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 476..528
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 546..763
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 782..901
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 936..1036
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 831
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 975
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1121 AA; 124534 MW; 1E63EAD24CBB568B CRC64;
MYSLNSFFVT NIDNAHLAMG DYNYLLVALS ILLASVASFF ALHFASIAQH IVIEKYKSIA
LVSGSFIMAG GIWSMHFVGM LAFNMGHGIS YDPLLTAISL IPAILASYIT LKRFIRSDLS
IWQLLINGVL VGGGIGAMHY IGMAAMKMDV ELKYDPAWFL ASLVIAVVLA FIALSTHYYV
RKVWANLTTK WVSCISALIM GAAISGMHYA GMAGARFISS SKAEMHHIQD STNDELSFVV
AIITLLLSIL AANIASQLRY RQLLLEKTAS EVRLKTTLDT AVDGIISIDS LGIIKEFNKA
ATKIFGWQEE EIINQHFGAL FPQKYTDEFN RSLAAFRNTG EVTIAGTERE IHAINKTGHI
FPIRLGVGKV DIPDSDTLFV GFITDISTRK SLEETIKKSE KQFSSLIKNI PGASFRCLMD
EHWTTIFVSD AIYDVTGWST SEFYSKTISF AKLVHPDDEE NVASTIKEAT NTRKSYKLEY
RLRHKDGHYV WVLENGSVIL NKHGKPEWID GVILDISQRV EMEDELRQAK AKAEASVESK
ASFLANMSHE IRTPMNAIIG FSDILLESEI SGENKKHLSI ISKSARSLLH LLNDILDSAK
LEKNKLELDI QPFVLANSVD TVISTLWLQA RNKGLELNFN IEKDVAVAYL GAEDRIRQVL
MNILGNAVKF TEKGHVTLNV LKLQDGKIRF SVTDSGIGIP EERLTHIFDP FTQADASMSR
RFGGTGLGTS ISKQLVTLMG GQIHVTSEAE VGSCFFFDLP LTETEAPSDT KTSQLSIIAP
QKILLADDVE QNLTLLTILL KRHGHAIFFA KDGIDAVEQF KMIKPDIILM DIQMPKMDGL
TATQIIRSYE KENQLIHTPI IALTANVLIE DKLDAQQAGM DGFANKPIDI QALITEMARV
LNEVPIQIDL KRLDHQKVNH KNPQIHMDKG LSLWNDLPVY ITELSRFAET NENLVNRLTT
HLDNQEYQEA YALAHAIKGS SGNLALLNIS NCMASIERAA QTKDHDQFSK NVQCLASLLA
YFFEELQLLI EKYSIHSEIS DASTQNEFST TQLIALIEAL ILSANSGEVD DENIALLIRN
APQYMKTQAI AASKAISNFE FDSAINSLTN LKALMIQEPT K
//
