ID A0A330L2Z1_9BACT Unreviewed; 886 AA.
AC A0A330L2Z1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NITLEN_100008 {ECO:0000313|EMBL:SPP64138.1};
OS Nitrospira lenta.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1436998 {ECO:0000313|EMBL:SPP64138.1, ECO:0000313|Proteomes:UP000248168};
RN [1] {ECO:0000313|Proteomes:UP000248168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucker S., Sakoula D.;
RL Submitted (APR-2018) 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; OUNR01000002; SPP64138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A330L2Z1; -.
DR InParanoid; A0A330L2Z1; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000248168; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 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 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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SPP64138.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000248168};
KW Transferase {ECO:0000313|EMBL:SPP64138.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 362..581
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 599..720
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 758..877
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 723..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 303..337
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 653
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 807
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 886 AA; 96988 MW; 82F819BCB97156B9 CRC64;
MAGPLQSLTL IDADTLVTAR IKNPGISTAR FVRHLWLILG LFAALAGQFA LYVQVQHEVA
EASAVRETAL QLAQELRQSS DDLTRMVRTY LTTGNPLYKK HFQEIIAIRN GTSPRPVDYH
HVYWDMVQLD DRRPTPMGPP EALLTKLAAV GVTDEELAKL KESMQRSDDL TTREFAAIAM
VEQHSPVPLS TRLAAINLVH DETYLQARSR IMAPIGEFAR LIDARTLNAV ERQQAHADRA
LWILIGIGML LVGVLYNTHR SLYHILGTTV DRLYTHMDRL GQGHFTEAIA LNPAQVPSIL
GRLAEAQRNL AALDGERRQA EEDLQQHQAR LETLVATRTA DLEIAKQAAE SASLAKSAFL
ACMSHEIRTP MNAIIGMTEL LQETALSEEQ QTYVDRFGRA TNALLSLIND ILDLSKIEAG
QMELECISFD LVDVIESVGE LMAQRASSKG LELILHLDPR LPRYVRGDPT RLRQIFVNLV
GNAVKFTVRG EIVLRAEPSL SESECLSFHV TDTGIGIPAD RVDHIFERFT QVDSSTTRQY
GGTGLGLSIS RHLAELMAGR IWATSTLGIG TTIHLTIPLP PAHTLTAAAP HLTMPVERRI
LIVDDNDTNR LALRTVLSQT GVIVSEARSG PEALTQLEDA RQNETLPHLL LLDCYMPDMD
GFVVAEALQA KPELAAIPSI LLTSDLRAGD RARATRAGIR RFLNKPIRRS ALLKTIDTLL
TDPRPESSAA SADVPAAAPA QAAPPAPPPV SPAQTTGRIL LAEDIEDNRE IVKLFLKSTG
YQVISVENGA LAVEHFQSAS VDLVLMDIQM PIMDGLTATA IIRAWEQQQG RPMTPIIALT
ANAFQEDITQ CLAAGCSAHL AKPIKKHALL SLIQACLTSA PSRQAA
//
