ID A0A1E2VAN2_9GAMM Unreviewed; 1315 AA.
AC A0A1E2VAN2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BFW38_10980 {ECO:0000313|EMBL:ODC03983.1};
OS Terasakiispira papahanaumokuakeensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Terasakiispira.
OX NCBI_TaxID=197479 {ECO:0000313|EMBL:ODC03983.1, ECO:0000313|Proteomes:UP000094291};
RN [1] {ECO:0000313|EMBL:ODC03983.1, ECO:0000313|Proteomes:UP000094291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH27A {ECO:0000313|EMBL:ODC03983.1,
RC ECO:0000313|Proteomes:UP000094291};
RA Seilhamer J.J.;
RL Submitted (AUG-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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000256|ARBA:ARBA00006434}.
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:ODC03983.1}.
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DR EMBL; MDTQ01000001; ODC03983.1; -; Genomic_DNA.
DR RefSeq; WP_068998690.1; NZ_MDTQ01000001.1.
DR STRING; 197479.BFW38_10980; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000094291; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd10322; SLC5sbd; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 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; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; NF041832; near_NosP_CTERM; 1.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ODC03983.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000094291};
KW Transferase {ECO:0000313|EMBL:ODC03983.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 776..846
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 848..900
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 957..1171
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1193..1310
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 902..950
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1244
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1315 AA; 146831 MW; 662306D3AABE678A CRC64;
MFAGWQLILV ALSYLMLLFG IAWWGDRRAL GRNSQKPRPF VYSLALAIYC TSWTFFGAVG
QAAEGGWVYL GIFLGPILAY VLGWRLIRKT LRASKAQNIT SIADFIASRY GKWQVLAVVV
TLVALIGSLP YIALQLKAVA MAYDMLIHYP APPPDHKQLP AVADTAFHVA IVMAIFAILF
GTRSINATEH HNGLVKAIAF EGVVKLLAFL AVGSFITYGV FSGFNDLMSK AQIYFDLQKT
LGSGDVPRGL IAQTLVSMFA ILMLPRQFHV TVVENTHQDD LKVSRWLLPL YLVLIALFVM
PIAAAGLILF SDGSVEPDVF MLALPLSLHS KELALVAFFG GFSAATSMSI MATVAISIMV
SNEIVIPFLL KSRWNNNTSH HDFGRVVLRI RRLTMLAVML LSYLTYRLVA EFNSLAATGL
LSFAAIAQLA PAVIGGLIWK RGNRWGALAG LVMGMWFWAY TLLIPSLQAA GLIDARLMSH
GPWDIQWLRP DALLGTGHLD FFTHGVFWSL GVNLLAYISI SRLTRQRVID RIQASAFVDN
IEARPAKIRR PWQGVTTVGD LKLLGQRFIG HDATNQAFDH YAHQRHLPPL RPEEKASIEL
IQFTERLLAG VLGASSARIV ISSTLQGKEI QIADVISIVD EASQVLEFSR GLLQSTVEHL
SQGISVVDQH QRLVVWNQRY LELFHFPDGF VQVGCPMVDV FRYNAENGEY GPGDPEAHVQ
QLMDNIRQGE PHRYTRYRQD GTVLDVQGNP MPGGGFVFSY QDITQQKQTE EALIQSENNI
RIYTDNVPAL IAYFDTEKRY LFTNRAYEEA MGIDRTEVIG QPIYKVLSEA QYEHRKPYMK
AALEGKLQSF ELELPSRNKG MRYALVTYTP HHAENGDVLG FFALYQDITE RRLVEIALQE
TNEHLEERVR ERTLALSELN AALLTENQVR AKAEEAMRQA KQQAEDANAS KTRFLAAASH
DLLQPLNAAR LFTSALAQRT HDDNTRATTE NIDNSLKAAE ELLSTLLDIS KLDAGAMQPK
ISHFALTDIL HPLKAEFSIM ASQRDLELDV IDSRSWVKSD PQMLRRIVQN FLSNAMRYTR
EGRVLLGCRR EGPHHLRIEV WDTGPGIPEA KQLEIFQEFR RLDTPDKHNE KGLGLGLSIA
ERMSRVMGHD LRVRSWPGQG TVFSITVEKG EVQQEQPVST SPRARMNKLD GVTVLCIDNE
PMILEGMSAM LSGWHCEVFT ATTIGGAKSI LRSQSEPPQV FLADYHLDNE VTGIMALKAL
EEALGEPVPG IVITADRTDE IAEEVQQAGY QLLHKPVKPA ALRALMTRTL QRNKP
//
