ID A0A1Y0G853_9PROT Unreviewed; 843 AA.
AC A0A1Y0G853;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CAP31_09895 {ECO:0000313|EMBL:ARU31962.1};
OS Sulfuriferula sp. AH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuriferula.
OX NCBI_TaxID=1985873 {ECO:0000313|EMBL:ARU31962.1, ECO:0000313|Proteomes:UP000195558};
RN [1] {ECO:0000313|EMBL:ARU31962.1, ECO:0000313|Proteomes:UP000195558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH1 {ECO:0000313|EMBL:ARU31962.1,
RC ECO:0000313|Proteomes:UP000195558};
RA Jones D.S., Hua A.A., Roepke E.W., Bailey J.V.;
RT "The complete genome sequence of Sulfuriferula sp. str. AH1, a sulfur-
RT oxidizing autotroph isolated from weathered sulfide-bearing rock from the
RT Duluth Complex.";
RL Submitted (MAY-2017) 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; CP021138; ARU31962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0G853; -.
DR KEGG; sulf:CAP31_09895; -.
DR OrthoDB; 8552871at2; -.
DR Proteomes; UP000195558; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 1.
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; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
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; PF12729; 4HB_MCP_1; 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; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 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 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:UP000195558};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 300..350
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 368..584
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 605..720
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 743..839
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 654
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 781
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 843 AA; 93561 MW; 53E42B078A353FD3 CRC64;
MKQINLKLSL AIGFGLMLAL LLALTLLGLA QMRSINAKLE TIVTVNNYKT ELITIMRDAL
RDRTITLHSL VLNTSPFDQN DELYEFHENS VRFGQALQAL NLSPLGPKEQ QRLAQISEYA
KIAQPLGVRT ADLALDQRNT EALFLLQHST IPAQKKILVA LDDLLALQRS ANADAAVAAF
NTYDQTRNFV IVMGTAAGLV GLLIAVFVTR RAGRQADEIE KQKLKYQTLF EANSDAIVII
GKNGFTDCNP AALAMFRIKT VDEFIRRPPH MLGAPIQADG RSAETVANEA ILRVRKEGYY
AFEWTGIRTN GQTFPAEIAM YAMRIEDQPM IQAIMRDITQ RRQTEQNLQQ ARDAALEAAR
IKAEFVANVS HEIRTPMNAI IGMSGLLLKT PLDATQHDYA HTVDNAAKTL LKLINDILDF
SKIEAGKLDI EHIAFNLHQH LRDTVQLFNL RATEKDLEYT LDIAADVPEF IFGDPWRIRQ
VLTNLIDNAI KFTSAGAVRI LVEFDQNLLI VRVEDNGIGI SDEAKSRLFQ AFSQADGSTT
RKYGGTGLGL TISKQLIELM GGEIGVNDHR TQGSCFWFSL PVMPAAAADV DSATPIIVPH
FANQRILVVD DNAINRKVMY HLLMSLGLQV DTAANGKEAV ERCIAQHYDL VLMDCQMPEM
DGFAATSTIR NVAPHTGAII AMTANTQPDT RDNCLIAGMQ DYLSKPVLEA DLIRLFEHWL
NTTGTATSPP LDIDKLRQLF RRDDALIREL LQLYLGTSAP LIEQLEQGIA ARNPAATRYA
HELKGAAAYI SALTTSMLCE AIEHAIKTND WESAEARISE LKAVFLETRN FIQQYLQTDI
ASL
//
