ID G7EP00_9GAMM Unreviewed; 940 AA.
AC G7EP00;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=P20311_0396 {ECO:0000313|EMBL:GAA62623.1};
OS Pseudoalteromonas sp. BSi20311.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=383911 {ECO:0000313|EMBL:GAA62623.1, ECO:0000313|Proteomes:UP000005146};
RN [1] {ECO:0000313|Proteomes:UP000005146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSi20311 {ECO:0000313|Proteomes:UP000005146};
RX PubMed=22275105; DOI=10.1128/JB.06427-11;
RA Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT ice.";
RL J. Bacteriol. 194:908-909(2012).
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 -!- 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:GAA62623.1}.
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DR EMBL; BADU01000015; GAA62623.1; -; Genomic_DNA.
DR RefSeq; WP_008109067.1; NZ_BADU01000015.1.
DR AlphaFoldDB; G7EP00; -.
DR Proteomes; UP000005146; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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 Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00028; TPR; 6.
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 SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS50005; TPR; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..940
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003493407"
FT TRANSMEM 422..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 144..177
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 184..217
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 484..701
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 725..839
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 851..940
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 774
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 890
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 940 AA; 106175 MW; F70B92D3FF11C47A CRC64;
MLTQLKRICF IGLLAVLSSA SNDALSNEQP SLFEQFNLEQ TWPEKHRLAT DILSNPDVPN
LQRITIYSDL AELAFAQSDL ANALKYFKLL EISSTLKDQP KLYFRAIKMQ GVVLYYQGLV
QQAVVDYNRA LNIAITLKNP IKQANLLSNI GLAYFDMYNM ELALDYYQQA KVIYEKEGSA
QDKADILHNI AGIYIRLSRY ESALEMYREV LKVFQELGDE DGVAQAYGNM GVAYTESRQY
QLALHYNQLA LRYYQSVNNA FQLSTKHTNL ATINLKLNKF DVAFYHANAG QQYAIEADNK
SLLAAALHVL SIVQFVQGDT QSAKQTSERS ITLAKEYNNG MRIKDGLGIE ALINASLGDY
EKALSLHQQY VDYQRSVNTE EASKAVSQFQ IQFESNQLNQ EIKQLKQQQY LQELQIAKRS
QLTFLLVIVA ILILITVIAV YKRRTEKQAK LKLTEQVEQR TKELQSVAQE LREANEVKSQ
FLANISHEIR TPLTAILAQT DDLISGLYKP EQLQDELRVI QRQSEHLKSL INDVLDLSKI
EANRLELNIS CFDVVQLIND IHAMFSPQTK AKGLSLVLEC QLDKSYFTRL DLTRVKQILI
NLCANAIKFT HKGQVTIGVS KTEQGLLFSI RDTGIGMSSS QLKLIFECFS QADNSISRRF
GGTGLGLSLS QQLAAMMGGY ISVQSEFKKG SEFSFYLPSV QVEEQKCYND QQAKSGDGER
LLSGKVVLAE DHSDNRKLIT RYLHSLGLEV IAVENGEQAV EQSLKLYPDL VLLDIQMPVM
DGISAFELLK QCGYEQPILA LTANAMSHEI DHYLSLGFSD YLAKPIDKES FYTVLAKYLN
AANTETPTEK NHVDMSDLVT SFQQSLAEES ELVEQHFKDA DYQALQKDSH RVLGAAQMFE
FKEIAIAAKA LDDELLQPQL NTQKLTILVN NLQALFKQYE
//
