ID A0A177L516_9BACI Unreviewed; 998 AA.
AC A0A177L516;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AWH49_15055 {ECO:0000313|EMBL:OAH60769.1};
OS Domibacillus aminovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=29332 {ECO:0000313|EMBL:OAH60769.1, ECO:0000313|Proteomes:UP000076935};
RN [1] {ECO:0000313|EMBL:OAH60769.1, ECO:0000313|Proteomes:UP000076935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1314 {ECO:0000313|EMBL:OAH60769.1,
RC ECO:0000313|Proteomes:UP000076935};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Investigation of taxonomic status of Bacillus aminovorans.";
RL Submitted (JAN-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAH60769.1}.
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DR EMBL; LQWY01000031; OAH60769.1; -; Genomic_DNA.
DR RefSeq; WP_063965808.1; NZ_LQWY01000031.1.
DR AlphaFoldDB; A0A177L516; -.
DR Proteomes; UP000076935; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
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; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 582..817
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 879..996
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 506..572
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 929
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 998 AA; 113042 MW; 8B24A171EC2F0AC0 CRC64;
MEKLRKPLIF ITIIYALIYY LFILFWSTNT LGMGIVAVTG PIIALIFLGV AIYHIKELEE
KRFWFIIFAA CFSYFIGEFM WVAMDYPFPS WANFFFNLFV ILYSLAILYK VYMKRRQYGS
IQLFFDSFII MTVLTTITWV YFLEPLLQYE TSTFHFILSL TYPAAHLGIL IGIVMLFVSY
KSTFPPIVLT INTAVVFIYT IAEFYYLYRA IYDNYNYLSL ITPVWNICVI LIGLSSFYGS
HIDVQSPQEE KNQAKKVHSI FIIIPYLSLM VLVILAIIKK EAILGIFIGG MVVLFFIVIR
QVITISENGT LVRQLKGRTE ELERLQIEQL ELKEAADEQS WLKTRIAEIA NMYPGISDLE
TLAHLFIRKV TPMVGASYGV FYVKQDEGNQ ERFQKLAAYA DHYENQKEVG ASSFQLGEGL
VGQCALENRI ISLHQVPEDY IKINSGLGKA SPSDVLIIPA EYKGEVLAVI ELASFTSFSD
QELMLLKEGM SNLGINIQSI LRQMKIEKLL QESQALTEEL QSQSEELQSQ QEELRTVNEQ
LEEQYEHSEQ KTREVEKVKD ALEEKAQQLT LSSQYKSEFL ANMSHELRTP LNSLLILAQT
LTDNIDGNLT DKQVSYAKTI YSSGNDLLHL INDILDIVKI EAGKTEVISK DVELTNVKEF
VEAQFTPVAR KKNIKLHVQL ASDLPEMIHT DKQRLQQILK NLLSNAFKFT EHGAVTLTME
KAKKGRFGEE QEDAFTQSNI EFVFSVKDTG IGIAAENQGI IFDAFKQADG TISRKYGGTG
LGLSISRELA HLLGGFIEVE SIGGDGSTFT LYLPHYQNIA SEEDQNIARK EIAISEAATA
TALLENPSTA PVASAEYPFQ TEDSWKQAQG RKALLEGKKI LVVDDDMRNV FALTTALESY
QVEVVFAENG KDGITVLQGN PDIDLVIMDI MMPEMDGFET IRVIRQLPEF QSVPIIALTA
KAMKNDRQEC IEAGASDYIS KPVNLDQLFS IIRVWLYR
//
