ID A0A1I1GKE5_9GAMM Unreviewed; 934 AA.
AC A0A1I1GKE5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05660443_1468 {ECO:0000313|EMBL:SFC11752.1};
OS Marinospirillum celere.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinospirillum.
OX NCBI_TaxID=1122252 {ECO:0000313|EMBL:SFC11752.1, ECO:0000313|Proteomes:UP000199058};
RN [1] {ECO:0000313|EMBL:SFC11752.1, ECO:0000313|Proteomes:UP000199058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18438 {ECO:0000313|EMBL:SFC11752.1,
RC ECO:0000313|Proteomes:UP000199058};
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};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; FOLH01000003; SFC11752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1GKE5; -.
DR STRING; 1122252.SAMN05660443_1468; -.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000199058; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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; 1.20.120.160; HPT 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; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR036641; HPT_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 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; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 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; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:SFC11752.1};
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:UP000199058};
KW Transferase {ECO:0000313|EMBL:SFC11752.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 295..522
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 537..652
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 680..797
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 827..924
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 729
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 866
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 934 AA; 104161 MW; E6D46E7E7100F627 CRC64;
MPLSLRNWLL ICCFLPVWLL ILLGGGWLLQ SYFSSLEEQL IERGRLTLKN LGPSLAVQLE
DTDRLPQLRS LSEQLLETAD VRAFSIYDRQ RSSLLHAGPS MRPLESSNQE LRWSNQSQLA
VEQETLRFIE PIYQLSSGRD LSRLQAGENS LLLGWAELEL SRTPTLLNKY RLLLMGGLLV
LLLFVLSLFL LLYLSRYLGQ RLDLATTSLG QIAEGEQPPS LPTSAIQELQ GLQQSIGSLT
GELSQREDQL LQSIEEVRED ASRSLETIEI KNIELDRARK DALRASRIKS EFLANMSHEI
RTPLNGIIGF SNLLSRTHLD VRQKEYLGHI LGASETMLGI INDILDFSKI EAGKLVLEEE
AVDLRELLDT SLAMLAPQAH RQNLDLLGLI YDDVPQLVKS DPLRLKQLLS NLVSNALKFT
EQGEVVVRIM LDDEEPGDLT VGHKSSLRIA VTDTGVGLNA AQRQKLFQAF SQADTSQTRQ
FGGTGLGLAI CKQLVQQMGG QIGMDSEVGE GSTFWFTLPL EVVEAAPEPQ PWLEGRKLAV
LETHRLTRQA WSHQLSNWGA EVITAESPEA LLQAVKEQPI DLALVGMNSD EAASSSWLNV
LEQVRSHQLS CLLLLNTSEP EVHARFRPKV SEHLLLKPLS GNRLKEALSI LLEQSLPKKY
LTSEQDENPF KLDKKQAVAK ILSVDDTPSN LLLLVTLLQQ LGYETCEART GQEAVEVVKQ
EPVDLILMDI QMPEMDGVEA TRRIRSLGHQ YRSLPIIALT AHAVAEERAG WLQAGLNDIL
IKPLNEKLLT DILHRWLGEN LSYPALEEVA VPCPVDRDLG VRLAAGRPEL ADELLGLLLA
SLEESKEAIE QALANEQEMA LIDAVHRLHG ASRYCGVPDL AQLTEALETQ LKAKQHRLVA
ISLEQLFQEI ERLLEWKQNG YRADWHTSSI TGSG
//
