ID Q2W7A5_MAGSA Unreviewed; 2123 AA.
AC Q2W7A5;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=amb1466 {ECO:0000313|EMBL:BAE50270.1};
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE50270.1, ECO:0000313|Proteomes:UP000007058};
RN [1] {ECO:0000313|EMBL:BAE50270.1, ECO:0000313|Proteomes:UP000007058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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; AP007255; BAE50270.1; -; Genomic_DNA.
DR STRING; 342108.amb1466; -.
DR KEGG; mag:amb1466; -.
DR HOGENOM; CLU_000445_34_2_5; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000007058}.
FT DOMAIN 9..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1981..2119
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 1460..1494
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2123 AA; 233278 MW; 661D8638A6963B06 CRC64;
MTDRFLATLR RTEVLCRDGD TVLWRAQAED AGAALVRVAA DEVPSVRVAA RLAHEFGLRG
CLDSDWAVRP QLLAGQGGRA ELVLEDPGGI VLDALLRHHS KSRSGEKGLA VEGFLVLALR
MAEALAKLHA AGLVHKGIKP GAMLVAPDGD SIRFTSFGFA SVLPRHQMPP EPIESIEGDL
AYMAPEQTGR MNRSVDCRSD LYSLGIVFFE MLAGRLPFDS NDPAELVHFH VARRPPPLSR
FREDVPVVVL EMVAKLLSKA AEDRYQTAKG LAADLRICLE DWRGTGAIAP FLLGANDRPD
RLVIPEKLYG REAELRQLLD AAGRVTGDGA LEVVFVAGYS GIGKSVLVGE LQKALVGSNT
FFATGKFDQY KRHIPYATWA QAFQGCVRQI LGLDDARLVK WRLAILDAVG QNGRLITDLI
PDLALLIGEQ PLVPELPPNE AQHRFFTTFR RFLARWATER HPLVLFLDDL QWIDPGSLKL
LEYLAGRSEL GHLLLVCAYR DNEVGPAHPL TLAKDAIRAR TRIEEIPLRP LSTGHLRQLV
AETLSCPAAR AQPLVEIIGG KTGGNPFFTI QFMHGLFEEQ LLSPGPEGWQ WDMERIAAKN
FTDNVVDLMV GKILRLPEKT QEVMRRLACL GNMVPVRKLA LVHDGAAETL DADLGDALRA
SYLVRRNDTI HFSHDRIQEA AYSLLPAGDR PAEHLRIARK LAAGLDPAGF DDAIFEIVGH
FTQGVELVSD PEERYRLGRW CALAGEKAKA SAAYVTAQTF FVQAMDLLPP DAWDHDYDRT
LWLYLERVTC ELLLGNFQQV DDLLPFVLER TRGNADRARA YRLLILRNQV AGRYGDAVDI
ALNVLGLFGL DCPASPAEVD QAVAQGRREA SANLRGREIG ALIDAPAMTD PEALAMIGIL
ADCLPCSFLA RPDLYGWLAL NGLNITLRQG NTGDSCSIYM GYAIVLVSEF GEIDESLQYA
DLALKLQETL SRPDLKGRIL VRSGVFINSR RNSFESSIEI LREGFVECQA AGDYSYAVYG
ALEMCWLTLE SGAHLDELDA ASVTYSAFAE QSRNIGLLNA LRAQKAFVSS LTGALDPTGY
LENGAEFLAA LTGAKFGTGV AYFHLMGQMV ALLRGEYLQA RDQSLKVAAS LKSITGWVAE
TTYHLLAVLT LSQLDLPVEE RRQEMLGHVD LLRRRAGDSP RNYGCRYSLA LAELARLDGD
VLEAQRRYEE AIASARDGGF LHLEAMAYES ASRFYREREM ALIAETYLRK ARDCYAQWGA
VDKVRRIESE QPELGAEHIQ SAKGSESPAQ AQNLDVISVV KASQAVSGEI ALDRLVETLL
RITVENAGAQ RGALIVDLNG TPTVVAQARI GDGAVSVESQ RRVPNGADLP EKVLNYVHRA
WKRVLLDDAL QDNDFSSDPY LRAGKVRSVL CLPMVKQSRL IGLLYLENSH VSHVFTADRV
AVLDLLASQA AISLENALLY EDLQRHRDDL ERTVAERTAQ LVEKKEQLDK ILNEQEIILE
NASLGIVVVK LTADGRRVIQ RANIAAGRLL GYAPGALEGM ETRAVWTSEE DFRLVGEAYK
LMAEGQTYSG EHAIRRRNGE RGVCKLVGAA ADPSDLSKGT IWLIEDITDR RAADAALRAA
KDLAEEMAAA FRDKSEQVAS LLDNSGQGFL SFGANLVVDS QYSRACETML GQSPAGKDVA
SLLFPDEAAK ADLLRLGVPE ALKEREPFKR ELYLSLLPTE VRLRDLILAI EYSVLESGHL
MLVLTDITEE RRLEDRVRSN HKILQMVVTA VTDSRDFFDS VNAFRRFTQA EIPALAHSPL
PPSGVLEGLY REVHTFKGTL NQFSFQYTPE ALHCLEGRLG EMRARKDGLS ADDIRAAVAA
VPLEPPFERD LSQLREIIGD DFLDRGERIT LTAEQVVQLE RLASDLLRGE AIDTAVPEIR
RLLVEIGFLR KTPLCDTLSG HRNTVAQVAA RLEKNVAPVE ISGGEDIWID PKTFAPFLRS
LAHVFRNAVT HGIEDPDSRL LAGKNESGRI TCKVGRTADS IHLSIADDGV GIDQGAVRTR
VVEAGLMPAE AVAAMTEAQV LDLIFLDSMT TNVHLDQFSG RGVGLAAVRA ETAKLGGTVA
VRTRPGQGTE FVFTLPFQGE GQG
//
