ID A0A1M4TWT1_9BACT Unreviewed; 1092 AA.
AC A0A1M4TWT1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444274_101500 {ECO:0000313|EMBL:SHE48961.1};
OS Mariniphaga anaerophila.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mariniphaga.
OX NCBI_TaxID=1484053 {ECO:0000313|EMBL:SHE48961.1, ECO:0000313|Proteomes:UP000184164};
RN [1] {ECO:0000313|EMBL:SHE48961.1, ECO:0000313|Proteomes:UP000184164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26910 {ECO:0000313|EMBL:SHE48961.1,
RC ECO:0000313|Proteomes:UP000184164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FQUM01000001; SHE48961.1; -; Genomic_DNA.
DR RefSeq; WP_072998585.1; NZ_FQUM01000001.1.
DR AlphaFoldDB; A0A1M4TWT1; -.
DR STRING; 1484053.SAMN05444274_101500; -.
DR OrthoDB; 717811at2; -.
DR Proteomes; UP000184164; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; 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; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 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; 4.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000184164};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..269
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 274..326
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 409..462
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 463..505
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 590..633
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 730..951
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 979..1092
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1028
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1092 AA; 124873 MW; C43EBC9E4955B4A4 CRC64;
MAETFINNAS LLIALSFFYA IIRWYKPKSE FYFQIISGIW FGLVAVAAMI MPYEYGPGTI
YDGRSVVLTL AGLWGGGYTA ILSILIAGIY RIYIGGVGLW AGLATIIFCS AVGLLFRLKF
KDKLSEVKFS VFWIIGVVAH IVMLASQMLV PGRHFLILKE IWLPVILFFP FAFALISRFF
QFIDRYMNSN QKIWEAKELY RTTLLSIGDA VISTDRNGNI SQMNNVAEEL TGWRFRDAKG
KDLKKIFKII NEESRQEVES PFDKVVKKGA VVGLSNHTLL ISKDGREIPI ADSGAPIKNS
NDDIIGVVLV FRDQTEEREQ QKKLKESEAK YREREFWLRE SQRVGKIGSY DLDIKNDHWS
ASEVLDEIFG ISKDIPHNLE SWLKIVHPEN KNELLDYFMN SVLKEKRSFE KEYRIIRQND
GAECWVMGHG ELIFNEAGEP VRMFGTIQDI TKRKQFEQKL KESEERFRKA ILSAPIPVMV
HDEAGNVITL SEGWNHFSGY HIEDIPTLKE WTRKAYGEKA EEIENYVNNI FKEDKTVFSG
EFEITTKNGE KRIWNFYTTP LGLSGNRNIM LSMAPDVTQR IKMKEQLEES ERSYRLLFEE
HTAAKFLIDP ETTEIVKANK AASVFYGWSI KELESMSIND INVLSNEDVN IAIGQARNNE
RIYFEFKHRL SNGEIKDVEV FSSQTEYKGK VLLHSIVHDV TEKKRLMNEL IDAKERAEES
DRLKSAFLAN MSHEIRTPLN GIVGFTNLLT NEKNLSELDK QSYFRIINKS TEGLLKIIND
ILDISRLETG KTVIEQKVFD VGKTLSSLYL IFNKKLKEAG KENVKLILNE FPQKVHLNTD
ENRLIQVFSN LLDNALRFTH NGNIKFGISE MKNGHVEFFT SDTGIGISKE KQQMVFESFT
QADSGMTRSY GGTGLGLTIV KKLVDLLGGK IVLESELGKG SRFSFSLPYL SLDDEQKEDE
QNDEKAQIAI YTKIDTKTKI LIVEDDEVSR FYFKQILSRH YKKLFFAETG EQALKLYSAE
SPDIVLMDIG LPDINGLEIV KRIREKDQEV KIIAQSAYAM TGDREKAFQA GCSDFITKPV
EVGLLLSKLF KN
//
