ID A0A418YKN0_9GAMM Unreviewed; 1933 AA.
AC A0A418YKN0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D1Z90_01940 {ECO:0000313|EMBL:RJG51516.1};
OS Motilimonas pumila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadales genera incertae sedis; Motilimonas.
OX NCBI_TaxID=2303987 {ECO:0000313|EMBL:RJG51516.1, ECO:0000313|Proteomes:UP000283255};
RN [1] {ECO:0000313|EMBL:RJG51516.1, ECO:0000313|Proteomes:UP000283255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLHSC7-2 {ECO:0000313|EMBL:RJG51516.1,
RC ECO:0000313|Proteomes:UP000283255};
RA Wang F.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RJG51516.1, ECO:0000313|Proteomes:UP000283255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLHSC7-2 {ECO:0000313|EMBL:RJG51516.1,
RC ECO:0000313|Proteomes:UP000283255};
RA Wang F.-Q., Ren L.-H., Lin Y.-W., Sun G.-H., Du Z.-J., Zhao J.-X.,
RA Liu X.-J., Liu L.-J.;
RT "Motilimonas pumilus sp. nov., isolated from the gut of sea cucumber
RT (Apostichopus japonicus).";
RL Submitted (JAN-2019) 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:RJG51516.1}.
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DR EMBL; QZCH01000001; RJG51516.1; -; Genomic_DNA.
DR Proteomes; UP000283255; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 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; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; IPR001638; Solute-binding_3/MltF_N.
DR InterPro; IPR015168; SsuA/THI5.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF09084; NMT1; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF158472; HAMP 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; SSF53850; Periplasmic binding protein-like II; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 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:0000256|ARBA:ARBA00022777};
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:UP000283255};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 736..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 770..792
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1013..1065
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1063..1134
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1208..1429
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1582..1698
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1755..1853
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1708..1728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1631
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1794
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1933 AA; 215048 MW; E38E1823059A1CDA CRC64;
MPSAKGDMQV FLQRLFFVLL TSLVAQSHLT WAEEAPSQPN EKVVIQLKWL HQFQFAGYYA
ALSQGYFKDE GLEVELRPRS GDQTPEESVL SGAAEYGVSD SGVVIAHLQG QPLVLVSQTF
QQSPLVLFSL AGNGLTTDNI VTPYDLAGKT VMLGKSSLNS AQIESLLQKT VGRSAIDVVP
HQFSHAPLLA GEVDAMSGYV TSSLFDFKSH DHDVNIIDPA DYGVNFYGDN LFTTEQEVKN
HPERVEKVKR AVEKGWQFAL RNPELIVQHI MSYYHHEGIS KERLLFEAQQ LSRFVQADFI
AIGSFDKQRY QKIAETYHWL GLVEQSEIND RFFFQSLWQA PLALENDHNS NASAKLRIGF
NSNRPPYLFS AGSSSGLEIE LVKAALVSQG ARLKPVQFEP QDFSFEQVHK LGLDAVVSDA
GLEKVEAYRS DPILHYSLRL YSLRSRPLKI TSIADMKPYK IGVFSQNTAV LGEEFMSLAE
AGSPSNVVHI AEPKQRLLAL SKGEVDAIVM EPHLMHWLMQ TELHQSGEQV LVNSYEIFPG
EYSTYLFFQH AEQQKVFNQG LAKVKTSGEF ARLVSQYRDP NFYVLTEYTQ NIGNIIKSLV
LNNESAQLQE LLQIFALAMP NIQRIEVEDA FTNQHEYRTE RLSGEGASFV IEYRLSEQET
ISGLLSDVGT IKVHYRLTDE VLSLPSLESL VTACFSCSEH DKAAIQAALE KLVEPEQRLE
ALQSKPTDHD DQAYDYVLKA LLLVFVIIAS LVLAAWFYRG LPTIPTVKEM LFLISFAIAG
MVLGIGFCVT YLNEGIREYT KLEASANSSL QLAQELKQSS KDLTRFARAF SVTGDVRYKT
YFNAVLAIRD GQLAHPLEYD LSYWDHVIAG DKPLDHQGEI YHLEDRFSSL DLSQAEIDQL
ALAKKESDWL SNIELIAMNA AVDGIYLDSE GELQRKAEPD QAFARELLYG RDYLEAVSRV
MKPLDKVISL MTSRLDLQLE EIQKRNRGIM ISIIILSLLT IAFSIYFFVL LRRRIIGPLV
RLEQGAKELA NGHYSYHIDI KSNDEIGSLA QAFNTMASSI QDRTAGLHSI INTATDGIIV
FDEHGEIREF SPAAEQIFAY PKPMMLGQSI YKLLPEDEQR VLRRYILGDK VGNKYSVSEF
AQEAMALRSD AVEFPMEISL VEAFVGGERL FTCFVRDIRM RKKLQQDILQ AKEMAEQANQ
AKSNFLANMS HEIRTPMNAI IGMSHLALET NLDPQQQNYI KKVNVSAQSL LGIINDILDF
SKIEAGKLDM ECIPFHLEDV FVQLNNLVGL NAKQKSLKLL FDIASDTPSQ LIGDPLRLGQ
VLVNLGNNAV KFTDSGEIVV RVSTAPLNDG KVELHFSVSD SGIGMSPSQL DLLFQSFSQA
DASTTRKFGG TGLGLAISKK LVEMMEGKIW AKSQAGLGSE FHFTVLLMPF EGEAYHKLSG
PRFDQENTAL VMVTSPLERQ IYLNQMSQMG LKAISLEHWG SLPSLVARKD IGFIIADSTA
VNDLTDSGIA LTGLTLAQLS QRLAPMEKLN GVTKTLQLDL PATSLQVSQF LAQMVGQDDF
SSEQLSEQVE LAQAQHLLAG CRVLVVEDNE INQELAVELL SGKHIEVVLA NHGQEAVELI
QQQAFDGVLM DCQMPIMDGF AATRFIRQEL AEIELPIIAM TANAMVGDRE KVLSAGMNDH
IAKPINVVDM FVTMAKWIKP SQPITAQPLV VEPNNEGSRD AVNDSNTRAS QSDIDSFLNI
DGIDTQFGLT TCQGNPVLYR KLLLKFAQFS QQFARDFSQA MASDDATASS RCAHSLKGVA
ANIGAMDIAQ QAEQLESDCD DGINEQQLQA QLKQLLPELE AVSTEIQQKL ALSQRDEPVS
ELSQEAFELV FNQLLALLAD DDTQASDVVA QLLPAPQLQG YQPQLDELAN AIDSYDFELA
VEKAEQLQRT LGL
//
