ID A0A177L7M4_9BACI Unreviewed; 655 AA.
AC A0A177L7M4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AWH49_13355 {ECO:0000313|EMBL:OAH61386.1};
OS Domibacillus aminovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=29332 {ECO:0000313|EMBL:OAH61386.1, ECO:0000313|Proteomes:UP000076935};
RN [1] {ECO:0000313|EMBL:OAH61386.1, ECO:0000313|Proteomes:UP000076935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1314 {ECO:0000313|EMBL:OAH61386.1,
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:OAH61386.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQWY01000021; OAH61386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177L7M4; -.
DR STRING; 29332.AWH48_00990; -.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 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; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 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 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 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..474
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 536..653
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 270..315
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 586
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 655 AA; 73639 MW; D35F8C0F2B020CDA CRC64;
MLIGLSSFFS DKVNNVPQKE NKLSKLFYIN QTILPFLSLI ILLFLALTKK EAILSFFIGG
AVLLCLIIIR QVITIFENDI LVRKLKERTE ELEIVQLQLM DLKDGAEEQS WLKTKIVEIA
TMYPGIDNVE TLARQLITKI TPMVRATYGA IYVKVDKGGF QKLAAYADNQ QDVGAKSFRL
GEGIAGQCAL ENRMISLNQI PEDYIKITSG LGSARPSYVT VIPAEFQEEV LAVIELASFE
SFSHLEEVLL QEVMSNLGIN IQSILGHMQV EKLLQESQAL TEELQSQSQE LQSQQEELRS
VNEQLEEQVE LNNVKEFVEA QFTPVARKKN IQLHVQIASD LSEVIHTDKQ RLQQILKNLL
SNAFKFTEHG AVTLTIEKAE KGMFSKEKED AFTHSNIEFV FSVKDTGIGI ATENQDIIFD
AFKQADGTIS RKYGGTGLGL SISRELAHLL GGFIEVESTE GYGSTFTLYL PHYQNIVKEE
DQNIARKEIA IFEAEAATTH LENSSTVPVV SAEYPFQAED SWKQINGRKA LLEGKKILVV
DDDMRNVFAL TTALESYQVE VMFAENGRDG ITVLQGNPDI DLVIMDIMMP EMDGFETIRV
IRQLPEFQSL PIIALTAKAM KNDRQQCIEA GASDYISKPV NLRQLFSIIQ VWLYR
//