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Database: UniProt
Entry: A0A1H6F4J1_9GAMM
LinkDB: A0A1H6F4J1_9GAMM
Original site: A0A1H6F4J1_9GAMM 
ID   A0A1H6F4J1_9GAMM        Unreviewed;       747 AA.
AC   A0A1H6F4J1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=arcB_5 {ECO:0000313|EMBL:SEH04483.1};
GN   ORFNames=MBHS_00329 {ECO:0000313|EMBL:SEH04483.1};
OS   Candidatus Venteria ishoeyi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Venteria.
OX   NCBI_TaxID=1899563 {ECO:0000313|EMBL:SEH04483.1, ECO:0000313|Proteomes:UP000236724};
RN   [1] {ECO:0000313|EMBL:SEH04483.1, ECO:0000313|Proteomes:UP000236724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBHS1 {ECO:0000313|EMBL:SEH04483.1};
RA   de Groot N.N.;
RL   Submitted (OCT-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};
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DR   EMBL; FMSV02000056; SEH04483.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6F4J1; -.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000236724; Unassembled WGS sequence.
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; cd00130; PAS; 1.
DR   CDD; cd17574; REC_OmpR; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
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; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000236724};
KW   Transferase {ECO:0000313|EMBL:SEH04483.1}.
FT   DOMAIN          108..154
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          181..233
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          251..473
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          498..611
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          619..736
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         547
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         668
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   747 AA;  84710 MW;  9556AF18B3E3AD22 CRC64;
     MSSTPLNQQL EQVFQELYQG QSIPAEKQAY LQQLCEQVET LAQEKLDIEI SLETMTEHAD
     SFEQQLVASR NNLEVQVKER THELAERNLQ MEKEIQERQR AEEAQRNHLS FLNTLLDSIS
     SPIFFKNLNG EYLGCNSAFA DLICQSKQYI IGRNATDLWP NHIATEDSNM DQLLFEQETA
     QSYEMFVASP QNEFHDFIVN KTLFHNAVGQ TSGLVAIMVD ITERKRAEEA LLKAKESAEQ
     ANRVKSAFLA NMSHELRTPL NAVIGYSEML AEDLDDMGHN ELVPDARKIY SSGRHLLGLI
     NDVLDISKIE AGKMDLYNET FEISHLINEV TNTVTPLIEK KNNSLEVVQH TDANAIHADL
     TKVRQILFNL LSNAAKFTED GLIRFEITQQ EQEGKEWIQF LIKDQGIGMT PKQISKLFQP
     FTQADTSTTR KYGGTGLGLT ITKRFAEMMG GRVTVDSTPG TGSCFTVNLP AYVTAIDAEE
     QTHQTEEEAY HSTYNNTHVL VIDDDAVVRD LLSNYLEKMG YQVTTASHGD EGLKLAQKLK
     PDAITLDIMM PGMDGWMVLS ALKNNPELVD IPVIVLSMME ERKLGYSLGA SEYLTKPIDR
     EQLHHVLQKY LMPNQAGQWI MLVEDDEVTR TMLANQLKKS GWQVQTAENG KVALEQLELV
     IPDLILSDLM MPEMDGFEFL RYLREKPEWQ NIPVIVLTAK DITPEDRLAL NQQVTRIFQK
     TSYHRDDLLQ ELSDCLAELP KSKTLLD
//
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