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Database: UniProt
Entry: A4U1M9_9PROT
LinkDB: A4U1M9_9PROT
Original site: A4U1M9_9PROT 
ID   A4U1M9_9PROT            Unreviewed;       830 AA.
AC   A4U1M9;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=MGR_3139 {ECO:0000313|EMBL:CAM76786.1};
OS   Magnetospirillum gryphiswaldense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM76786.1};
RN   [1] {ECO:0000313|EMBL:CAM76786.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MSR-1 {ECO:0000313|EMBL:CAM76786.1};
RX   PubMed=17449609; DOI=10.1128/JB.00119-07;
RA   Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA   Reinhardt R., Schueler D.;
RT   "Comparative genome analysis of four magnetotactic bacteria reveals a
RT   complex set of group-specific genes implicated in magnetosome
RT   biomineralization and function.";
RL   J. Bacteriol. 189:4899-4910(2007).
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CU459003; CAM76786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4U1M9; -.
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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
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   PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CAM76786.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:CAM76786.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          598..818
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          553..584
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   830 AA;  90139 MW;  9BF0F2260B507090 CRC64;
     MAGGTVVAVI LWFGLDMVQS ARTDAIIHAN VDHQLKVQAE AGQARFQAIL QNHFTYTAFL
     AASAPVSDLA GQSLRFSPTE KPVDGLLSEL SLLHDPISRA DISFLAVIDG NSRIRRLMSD
     GAHPPPAGLQ DFVAALPVNA AHRAIVQRLG GDVYVVSVHA IAGQRASLVV LTRWDSGLLT
     RAHGFAPGSD LTVAIADMFH GVVAASSDPA VIAMGLPLIR LETDWLAVYQ ELPDHGGIDF
     LPAFVTIVSH AYADRQAEPL LRQEREQRTV LAATLIGLFL LVLVVVALRL RQIIDQVALV
     IESVNGKQEP AFKGGDELLG LVRQVHTLAT EVRRSRQALQ SEAAEKMRLN EERILVREEN
     ARLRLLQTVT DLLRVGVVRL GHDGPVAENR AMEEMSQTCG GLSPFVQASN RGSQDLVALD
     THGAERIYEL LSADGIDHDL ILVTEVTEQR RAEQMIHSLA LFPAQSPYPV LRIGIDGAIL
     HANPASEPLL SEWATGMGRK VPDEWHGIIT EVLATGRQLQ AELPVIGRVL SLTLVPVKGA
     GYVNIYATDV SDRVAAERQL ADANEDLERR VEERTRDLVR AKEQAELASR SKSEFLATIS
     HELRTPLNAI IGFSEVMAGS MFGPLGNSRY QEYAGDIVQS GRHLLAVIND ILDVSKIEAG
     QMSLDFGPVD IPPVIDSAVR LVETRARANS LRLRSEVDKD LPIIDGDRRR CLQILVNLLS
     NAIKFTPEGG QVTIGASREN DGIRLKVQDT GIGMSESEIQ VALEPFRQVD GSLSRQYEGT
     GLGLPLAKSM VELHGGSLVV NSRKGEGTEV AFWLPLNQNS GKGLGPNWDI
//
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