ID A0A1B7UQV3_9GAMM Unreviewed; 2194 AA.
AC A0A1B7UQV3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A5320_05430 {ECO:0000313|EMBL:OBP16814.1};
OS Rheinheimera sp. SA_1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1827365 {ECO:0000313|EMBL:OBP16814.1, ECO:0000313|Proteomes:UP000092258};
RN [1] {ECO:0000313|EMBL:OBP16814.1, ECO:0000313|Proteomes:UP000092258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA_1 {ECO:0000313|EMBL:OBP16814.1,
RC ECO:0000313|Proteomes:UP000092258};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-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:OBP16814.1}.
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DR EMBL; LXWK01000011; OBP16814.1; -; Genomic_DNA.
DR RefSeq; WP_068062530.1; NZ_LXWK01000011.1.
DR STRING; 1827365.A5320_05430; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000092258; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PF13191; AAA_16; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000092258};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..254
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1482..1703
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1721..1840
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1862..1978
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 2024..2115
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1775
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1911
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 2063
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 2194 AA; 245473 MW; D89FBF94767E34B3 CRC64;
MLSLQNFTDV QEQSALSAYV RLFSASLHGQ QLLIKQMDKN RPLPQFDLQE LQPQLPAPIH
SWSDNQYDYQ SFSATALPEQ LSQVLGNLAA ANLGVQLQWM LQLTLLLESL HQRQLVLGDL
RACAVFRCAN SRSLVLLDVS QAAAISSVNS LKLHQYDDLN ALRTIAPEAT GRVNAPLDQR
TDLYSLGVLF YAIVAGRYPF EQQQPIELVH AHIALTPPPL PLIPAPLNLL ISTLLQKNSN
QRYSQISGLR HDLELLLNQW QQQQQLELPE LSLRLGDQQL HFSSQLYGRE TQQAQLQALY
QQVRQQQQNQ LLLIEGYSGI GKTALIDQLY RHTLIERPHF CRGKFDQYQR NQLYSAWQQL
LTDLSEQLLQ EPAAQLQTWQ QQLQQVLGGQ ISVLQALIPS LQPLLGEPQT KATPPGTETG
FNASVDPGID QLLLQFFRVM GQICSQSKRP LVLLLDDVQW ADNSSLRLLQ ALLTDDGVRG
ILLILSYRDN EMDEVHPLRH ILQKLQQAGV EPQRIELQSL DQNAVTAWLA DTLRQPPAQL
HDFSQLLIEK TSGNPFFLRQ FLLMLQQKNL LVCDDKGRWS WDINAIARQN ITDNLVELTA
QRFATLSPGA HQLLKVAALL GETADLQVLA AVLQQSYPAL QPVIGEVVHT GIMTAYSQQH
GAQISSLRFV HDRLQQAAFA LLQDDATALH RAIADYYLQG RSEAEQQQNL FSYIDHLNAA
GDNAVSHYGA LAVAQLNLAA ARQAHAGNAW HEAAAYYQRA YNLSGQADDT PTPTTTQLRF
DSLLGMANCQ YLTQQYDAAD QSCLQLHQAA DLPLPRMQVA RLEILLLFAR NNFAPAFELA
QQVLQPVGVD ISQLDDIPVR YLELEQLYDK TRISDLVQQP ALTSAELLMA MEILNTLLTV
AYLVSPLHYL AVSYALVSLS IQNGHCAASS KAYSTHAMNL SGAFGQYKEA LDFADLAIVV
NQQYQGKFAP ELNFQRAATV LHWNAPLQKS LQALEQNTYL ALGQGNLEYA VHSALFFSFY
QSLSGTSLDE VAINLQKYRQ FISEKKFAYN LEYIRLWQQY VLNLQMSDLQ ASEGDVLLLS
GEAFNEAEQL PLLEQTNNVT ILFCYHSIKL MLAYLFNDDE AAIRHYQAAL PLTGVAMSLY
HQTEFYFFAA LLATRLCQQQ PEQQSQWQPL AEQYLQLLQQ WSRRASANHQ HKVALLEAEL
AAIAKQPLAW QAYDQALKLA QQSGFCQHHA IAAELTAGYW QRLGKADFAS LHWQQALQQY
QNWQAHRKVA QLQQLQPQLQ TKPQNQLLDM ASVLKAAETL SGQIDLSAFL QQMIELIVEN
AGAQAGRLWL LDEQQQLQLK ASAPATSASR AMSGQLLALV SRTLQPRLVN DLAGSGSLFQ
DLPQPLPAAV LCIPVIVSGQ LCGLLYLEHF ELSGAFTEDR INLLQLLANQ TAILSENTRL
YHQVVAANKN LEQKVWERTQ ELASAKIKAE SATAAKSSFL ARMSHEIRTP INAVIGLSRL
ANKTSLTLEQ QDYLSKIQES GEVLLSLVND ILDFSKIEAG KLELEISRFS LDKVLQRSVN
LNALKAHAKS LELICNVDPA LPAMLMGDPL RIQQILVNLI SNAVKFSDRG VIGIQVKLLQ
QQDNQLSLQL AISDNGIGIT PEQQQGLFQS FSQADDSITR KYGGSGLGLA ICKQLCELMG
GKIWLESQYG HGTTFYCQLQ VQSADIQQST ALLPLDISKL KALVVDDITL ARTVLLSLLG
EMGISADQTD NGYQAIEMVR QAKAAAQPYD FVLMDWRMPG IDGIETSRRI QQLDDAPHIL
MVSAYDREQA RASLQDVKIS QFIEKPVNQS ILLDALYTML EQDMPRRQVT DISDIPDLAR
YRILLVEDHA INRQVALGLL KDSQVQVDIA ENGLLAIHRL QQQRYDLVLM DIQMPEMDGL
TACQHIRQQL LLTELPVIAM TAHAMASDIA KSKAAGMNDH LTKPIDPQQL YSTLLQYLPA
EPHARRPAPI VATGPTLAEQ QQWQQLNECS AIDADRALKN LGGKLSLYLK LIDDFQQEHQ
QQSSKLQSMF RHQQWQPLYL DIHSLKSTSA YIGAFEFSQL CQQFETTLSQ QTATAEALQL
LCDQLQLLMQ QLSKVSPTAP QQIQFQHLTE ALTTLLPLLQ ESDFAAEDLL PALLEVASHH
PHVLMVEQIA ADIRQVEYEK AAGQTVQLLQ QLLQ
//
