ID A1SZV1_PSYIN Unreviewed; 968 AA.
AC A1SZV1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Ping_3329 {ECO:0000313|EMBL:ABM05016.1};
OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM05016.1, ECO:0000313|Proteomes:UP000000639};
RN [1] {ECO:0000313|EMBL:ABM05016.1, ECO:0000313|Proteomes:UP000000639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37 {ECO:0000313|EMBL:ABM05016.1,
RC ECO:0000313|Proteomes:UP000000639};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-2007) 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}.
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DR EMBL; CP000510; ABM05016.1; -; Genomic_DNA.
DR RefSeq; WP_011771568.1; NC_008709.1.
DR AlphaFoldDB; A1SZV1; -.
DR STRING; 357804.Ping_3329; -.
DR KEGG; pin:Ping_3329; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG4564; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_012936_0_0_6; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000000639; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd18774; PDC2_HK_sensor; 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; 6.10.340.10; -; 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; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR004010; Double_Cache_2.
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; IPR033480; sCache_2.
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; PF08269; dCache_2; 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; SM01049; Cache_2; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 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 Kinase {ECO:0000313|EMBL:ABM05016.1};
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:UP000000639};
KW Transferase {ECO:0000313|EMBL:ABM05016.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 344..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 445..666
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 691..810
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 860..960
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 740
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 899
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 968 AA; 108258 MW; 6B513E11761F8668 CRC64;
MIFTSLKFKV VALILLVLVI TSAATLYFTQ RDVGSAMLRA EQSSAENVLQ LAELNIRSSY
DQLISDKIEL LTQLKKEMVQ TAKVSNSVLH EFMLLSQGGR LSKEEAQQRA KRWLSKVDYP
SGDIFLFDHK GTILSSSQSK LNGVAITDIR DVKGRLIYDA MRDDQLEPRG DTAIFSWQKP
WQTKPSQFMG QFLPVNGWSW TLAVVVNFDN VEQESQRKMD SIIATLTQTF TKIQIAKTGY
AFLFDGDKKI LIAPPEDNLD NLDNLDKFKD TSGWLPRYSS VLDKIIAVNG KNKSAISYND
PFSGDREVEV FTSYFKAFDW YLGVVVPMAE IKAPGKNLIK RQSIIIALIS LVGLAAALLL
VFRISRPLNT LASYAKALPT QDFSQQNPDT IKIKRLAMKY SDEVGRLAES FVFMEASIRK
NIQQALHEKE IAVKASQAKS EFLATMSHEI RTPMNGVLGM TELVLETELS SEQRRFMEMI
KSSGFGLLDI INDILDFSKI EAGKLQLDNH PMQLQELIKH LVTSLSPLAK KKGLQLNYNL
PQEMDTWVLG DRIRLRQVLT NLISNAIKFT QRGEVLVSAV IFEQSATALS LQIRVRDSGI
GIAPENQDKI FESFSQADSS TTRNYGGTGL GLAISKQLIE MMGGSIGFSS ELGQGTTFWF
DLKLKPTEQI LSDETLPVST LEQQQITLQG KILLVEDHPV NQEFAMQILS GLGVDLHLAG
NGVEALKQLK EQNYDLVLMD CQMPVMDGYR ATELIRQKEQ ENGSPRLPII ALTANAMIED
RQRCISAGMD DYLSKPFNKA QIVVLLQRWL SADSGLMAVV EPEMAVEKAT ATKVIEPEIA
VSNEPLLPAI IAQLQEMDDN DGFFNRIVDA YLEKSPADIE QLNQGLARSD PEALRKAAHS
FKSSSYNLGA HKLAELCKTL EKRVRDKDLE EAASLCVSID GEYQRVRMAL IKIKENNNAE
NSDEQWSH
//
