ID V6F150_MAGGM Unreviewed; 891 AA.
AC V6F150;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MGMSRv2__1902 {ECO:0000313|EMBL:CDK99117.1};
OS Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS / MSR-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=431944 {ECO:0000313|EMBL:CDK99117.1, ECO:0000313|Proteomes:UP000018922};
RN [1] {ECO:0000313|EMBL:CDK99117.1, ECO:0000313|Proteomes:UP000018922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1
RC {ECO:0000313|Proteomes:UP000018922};
RX PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA Wang L., Li J.;
RT "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL Genome Announc. 2:e00171-e00114(2014).
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; HG794546; CDK99117.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F150; -.
DR STRING; 1430440.MGMSRv2__1902; -.
DR KEGG; mgy:MGMSRv2__1902; -.
DR eggNOG; COG4251; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000445_114_21_5; -.
DR Proteomes; UP000018922; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR003660; HAMP_dom.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDK99117.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018922};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..392
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 400..445
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 473..525
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 522..568
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 595..647
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 665..877
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 891 AA; 98359 MW; A56C082B581A8338 CRC64;
MTGHGFDDQG KSLLSPAAKS SASFDSRLGL RVRLGLTVGG LACGLALAIG LLFAELARNH
LAERQGQALS GLAAQILDAL DRGMFERFRE IQILAELDEF RSPATPVDSK RRILERVQST
YQYYAWIGIA DLASGQGLVG TQGYLETRDL SKRPWFSEGA KAPYVGDVHD ALLLAKLLPN
PRGAPIYLLD VATPIRDPDG NVVQVLCGHL HWWWTQDVVN TFNKPTDTQI FLISREGIVL
IGTTGNEGEA FSRIAPAGMD LASVNRAGDL LRWQDGTIYL SGFARSQGYQ SYPGLGWTII
VRQNESTALA LARATRERIL WIGGIAGLLG AIVGWQLAGR LAAPIERLSA AAARIGEGAL
TEPIPLVSGY REVATLARSL SGMVNSLTTE IAERRAAEAQ LKLAATVFRS SSEGILITDA
ANTVVAVNDS FFAITGYRRE EILGQRPSIL GSGRHGPDFY ISMWQTLAAT GGWQGEIWNR
RKNGEIYPEW LSIKAVSDEN GRLANYVAVF RDITDIRKAD EAIRKLQRAV EQSPVAIIIT
DTAANIEYVN PQFTLNTGYS FEDVVGRNPR ILRDGGKSDA EYKALWETIS SGRTWTGEFC
NRRKDGSTYW EEAIIAPIRN AEGGITHYVA IKEDVTARKK AERELMQTLD LVTRQNSELE
RFAYVAAHDL QEPLRTITAF TQLIERQMSE RLTVEEKDWM GLVSSAALRM YSLINDLLIY
SRIAADTPLK IIDMGVCCRE ALDNVRQSLE ATGGTVTVEP LPKVHGDHRQ MVQLWQNLLG
NSIKFHNPLR PLAIRVQARE DGGVWEFSVT DNGIGIEDSE HDMFDLFRRQ HTAEKYPGTG
IGLTICKRIV MHHGGRIWFQ ARPNEGCTFF FTIHSSVAVE LEGAGGFPET S
//
