ID A0A0F4QLA7_9GAMM Unreviewed; 977 AA.
AC A0A0F4QLA7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TW77_13580 {ECO:0000313|EMBL:KJZ08055.1};
OS Pseudoalteromonas rubra.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ08055.1, ECO:0000313|Proteomes:UP000033452};
RN [1] {ECO:0000313|EMBL:KJZ08055.1, ECO:0000313|Proteomes:UP000033452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ08055.1,
RC ECO:0000313|Proteomes:UP000033452};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ08055.1}.
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DR EMBL; JXYA01000029; KJZ08055.1; -; Genomic_DNA.
DR RefSeq; WP_046005528.1; NZ_JXYA01000029.1.
DR AlphaFoldDB; A0A0F4QLA7; -.
DR PATRIC; fig|43658.5.peg.2866; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000033452; Unassembled WGS sequence.
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 CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT domain; 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; IPR036641; HPT_dom_sf.
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 PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
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}; Kinase {ECO:0000313|EMBL:KJZ08055.1};
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:UP000033452};
KW Transferase {ECO:0000313|EMBL:KJZ08055.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 284..510
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 666..787
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 876..971
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 789..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 183..259
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 789..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 715
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 915
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 977 AA; 108021 MW; E3E1B7B46423BE8D CRC64;
MENSSQTQIK GFVPLFIVVT IIIAAISAAA AFTWPDKHQS NTDTSQRPDL VLLAKDIATP
LSHSMMKLGY NYAKQILSAF EASNPEIELY LYSDSGIGQA SLVYQTNEQS ITPIKRQAKV
DQGGELVVHQ PLVLDDLPVG ELILRYAPKQ PVSNATPMTS IILAGCALLL TIAFGIFLKR
QIIGRLSKDL NELNEELQHL LAQKSYDIHV TEKLSFGLSK TAVGINQLIN QIRDIIQGNQ
AAQRELKQLQ TSLESEVQAR TLALEKATLN AERASEAKTT FLATMSHEIR TPMNGVIGTI
DLLRQTELDG AQHRLTTIIR DSAFSLLGIL DDILDFSKIE AGKLQMDNSV FSVAETIEEV
ARVLSSVARK RKLDLQLAIA PDIPNNLVGD AVRVRQVLYN LCSNAIKFTT TDDTRRGFVK
IAVEVAQNTS EHYTLRFTVT DNGKGMTQAQ LREIFNPFIQ AEGSITREYG GTGLGLSICK
SLVELMLGSI HVSSDIGMGS EFVVELPFSV KGQIAYANKA VLNGQRIAVL THEHARRNIV
ARYLSFMGAD TVVLREADEL SEYQYDSDVI WVLDGLDGMD KVNGQLRDLL YSIEHNNQQV
IVLSTMDEPA LNHDRIFYLN AAPLCKSSFM TAILVAAGLH QPKKLKPSRS LNKYLNVDDA
RAANKLVLLV EDNVLNQQVL TDQLHLLGYG VEVAENGEEG LARWQQAHYP IILTDLHMPK
MSGYDMVAKI REEAEQAADI NAQPYIIAIT ANALKGERDR CLAAGMNDYI TKPVELNVLE
ATLETWQKSA GKPAQVQTEN KATPVPTAAQ EPVTQSQAPA KPDTADNEHQ APAETAEPVD
DSSDAQPVAE QAPEPQQTAP EEPIDLAQLD KYVNHDANKR LRFFRMYLEQ SSELARDING
AVISMSQEEI VEACHQLKSI SKTIGAHRVA DVAAEFEQRC KGEELSSDDL IHLRDTLETH
YQQATEFIQR YLQSQVE
//
