ID A0A178MNR5_9PROT Unreviewed; 1092 AA.
AC A0A178MNR5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A6A04_18290 {ECO:0000313|EMBL:OAN50430.1};
OS Paramagnetospirillum marisnigri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=1285242 {ECO:0000313|EMBL:OAN50430.1, ECO:0000313|Proteomes:UP000078428};
RN [1] {ECO:0000313|EMBL:OAN50430.1, ECO:0000313|Proteomes:UP000078428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-1 {ECO:0000313|EMBL:OAN50430.1,
RC ECO:0000313|Proteomes:UP000078428};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:OAN50430.1}.
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DR EMBL; LWQT01000054; OAN50430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178MNR5; -.
DR STRING; 1285242.A6A04_18290; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000078428; Unassembled WGS sequence.
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; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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 Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000078428}.
FT DOMAIN 66..114
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 261..313
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 321..369
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 394..445
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 463..684
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 699..817
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 845..962
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 994..1092
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 304..331
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 753
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 894
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1033
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1092 AA; 119821 MW; 11F08AA4652626A4 CRC64;
MHRLLQRQLT RASRGSADGA PDFDLLMKLV SETYEEQDRE RRLNDRSTRL MEEELRAANL
ASRQQAEAHL QAILDTVGEG IVITDPTGHI LSVNPALLSV FGYERDELVG KAILALLPTK
GVSDANECAI QRIRELGRES YARRKNGECF PVELALGDLS PTGVEHFICI IRDISERKRI
EREMRMSELR FRDFAESSSD WFWETGADLR FTRFSGNFTE HTRVLPDHYV GKTRDEMVSD
ETDPEVRRQN LEDLKARRPF RGFVYRTKAM NGPGRVLRVN GKPVFTESGE FIGYRGTASD
ITEEIDAEER LKAAQAEMER LAQRNASILE SVDDGIFGID LNGKATFVNR AAAELLGYEP
AELVGADILP MIASNLETAD NLYGVLLRLT ASFRDDSASF KRSDGVALPV EYIASPVMEN
TRQVGVVIGF RDITQRRQVE RELREAKEAA EAGNRSKSEF LATMSHEIRT PMNGVIGMTG
LLLDTELDDE QRHFAETIRD SGESLLTVIN DILDFSKMEA GKLDLDFTEF ELPPLVESVV
DILAPRAHAK GIEIASLIPP DLRVMVRGDP GRLRQVLMNL TGNAVKFTEK GGVSIELRTL
DLTDGRAMIR FEVKDTGIGI AKEAQGRLFS MFQQVDSSTA RRYGGTGLGL AISRRLANLM
GGDVGLDSEP GRGSRFWIDL PLVVLGPQGL LPPDLRGCRV LVVDDNAVNR NVLERQLRAF
GVDVRACHDA GSGMNEMTRA AADGRPWQVA LIDAQMPIVS GTDMVRMIRA IPMLTATKVI
ITSSQGVVER DESCPIDAFL HKPLRQNTVL DTIARLLGLL ERQAPTRPAA TPEAPADTAT
AKRLRILVAE DNPVNQQVAL GLLRKLGHSV DVVGDGAEAV EAVRLLPYDL VLMDVQMPEM
DGLEATRVIR RLPSQSSQVP IVAMTANAMR GDDQICLDAG MNGYISKPID RQKLAEVLAR
YSGEAERKPV SPPLPTAGPS VDFSVLDLLK DDLEAETVVA ILAKFMEDAR ARVATSSDAL
AQGDFERVRR EAHTIKGAAA SLGLSAIRDG CLTLENTARA GDGCDVALAS LNQAVEALPA
TLSSTVYALP EG
//
