ID A0A3L8Q2C5_9GAMM Unreviewed; 1230 AA.
AC A0A3L8Q2C5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D5018_04585 {ECO:0000313|EMBL:RLV60923.1};
OS Parashewanella curva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Parashewanella.
OX NCBI_TaxID=2338552 {ECO:0000313|EMBL:RLV60923.1, ECO:0000313|Proteomes:UP000281474};
RN [1] {ECO:0000313|EMBL:RLV60923.1, ECO:0000313|Proteomes:UP000281474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C51 {ECO:0000313|EMBL:RLV60923.1,
RC ECO:0000313|Proteomes:UP000281474};
RA Wang G.;
RT "Phylogeny of the Shewanellaceae, and recommendation for two new genera,
RT Pseudoshewanella and Parashewanella.";
RL Submitted (SEP-2018) 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 -!- 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:RLV60923.1}.
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DR EMBL; QZEI01000010; RLV60923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8Q2C5; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000281474; 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; cd00130; PAS; 2.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; 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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
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; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
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; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000281474};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 456..526
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 581..653
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 657..710
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 728..949
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 968..1088
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1111..1227
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 421..448
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1017
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1160
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1230 AA; 140315 MW; 9F41E0EBA2D89F26 CRC64;
MNPNEPAQQL TSPIQKSYNW AVFYTYFGVI IIAMLLSWSA YDSQKKEVIQ KRELQIEQHV
RQVDLLLESS IRAINSLRNV AVDHLRRGEL VRKDRMSEYE KFNETRQFFT LEPHYAKSGQ
PFTNMGRITG TGSLKNRSDR FYQELEMLFE LSLSFPVAKQ ATPESSSIYY ISKRKMMSYY
PWPSNEQRFR EELLNNKQFQ LAGPKMNPQR NVFWSEGYLG GVSKELLTTV GVPVYLDNEF
IGSINLDMTL SSLSKQIDDY FKMPGTVILL DQKNNVLSDS SMETGGMNRV FHLSQRIPAK
LHDISESELF DADEGFIRNG YYIQTVALQN VPWRLLYVQP VEAMFQEAKN EVEMTFIFVV
FALSVLVTIV HWLTRRSFVA PASQLLSHLE NCSQLPRPVP DKMSPGWAPW FQLVSRIFDE
NQQYTRNLSE QNKRLDKLVA NRTEKLKETT ERREREYALL RSLIDSIPEA IIFKDKEGKY
LGCNKAAERM LGYTENELIG QTSATLTNPE LGERIRAEDE QILKDKIPMR YQEKVELFGK
QVLLDTLKLP FYNRRNELLG LIAVWRDVTR EHESAEQLRL SEERYHLAMD AVEDGLWDWY
LDSEQIICNP AFYTMMGYKP NEFPALVSTI DDLIHPDDQQ RVQEYREQYL QAPDSVYEIE
YRMQAKNGEY YWLLSRGRVV EFTASGLPKR MVGTHKDITR QKINEVALLE AKQDAESANL
YKSEFLANMS HEIRTPMNAV IGMLELAQRT SLTEQQRDYL HKAGFSAQSL LRIINDILDF
SKIEAGKLEL EKVSFALDKV LDHAVDLNAI KAQEKGVELL LYAPVTAGLT LQGDPLRLGQ
VLINLLSNAV KFTQEGEIEL GCEDLGERDN RITLRFWVRD TGIGIEKTKQ ETLFDAFAQA
DGSTTRKYGG TGLGLSISQH LVSMMGGKME VESEPGNGST FSFTLSFEIA DDVKPDLKAL
PESLSSLKTL VVDDNPTALQ IYSNIMQDFN FDVQTVDNGE AALEQLQKQD IDLLLIDWMM
PNMHGGEVIE EVERMLEDGR IQHRPVIIMM TAHAQEPTQD EVDNTKVFTF LQKPFKASAL
FDAIVDAFAQ KESQESLELQ APAEIPTSKG KVLLVEDNLI NQQVASELLK SADYEVEIAE
NGQVALDMIA QNSYQAVLMD IQMPVMDGLT AAKKLRETYS ATELPIIAMT AHAMSGDREK
SLSAGMNAHI TKPIILNELF DTLAEWIKTS
//
