ID A0A1A7R869_9GAMM Unreviewed; 1517 AA.
AC A0A1A7R869;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A9J31_05110 {ECO:0000313|EMBL:OBX28455.1};
OS Acinetobacter gandensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1443941 {ECO:0000313|EMBL:OBX28455.1, ECO:0000313|Proteomes:UP000185753};
RN [1] {ECO:0000313|EMBL:OBX28455.1, ECO:0000313|Proteomes:UP000185753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4275 {ECO:0000313|EMBL:OBX28455.1,
RC ECO:0000313|Proteomes:UP000185753};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
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:OBX28455.1}.
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DR EMBL; LZDS01000025; OBX28455.1; -; Genomic_DNA.
DR RefSeq; WP_067764553.1; NZ_VZOF01000001.1.
DR STRING; 1443941.A9J31_05110; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000185753; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 4.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; 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 PANTHER; PTHR43395:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 4.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 4.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 4.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:OBX28455.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:OBX28455.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 19..123
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 205..309
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 534..638
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 738..856
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 998..1231
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1233..1374
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1396..1512
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 939..966
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 66
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 249
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 581
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 785
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1445
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1517 AA; 169409 MW; 246D0698C6C63636 CRC64;
MKEILKNLVE TTTLPEDSYL DQDAEILEIF VEEIEEIFAE LDGLFTTWLD NPQDKETLTT
IRRHFHTLKG SGRMVGAKSA GESAWAVEDT LNRVIAGSVQ LTPTVQKFAK TVLNVYQYKL
YPRFKNVAEL DVDLRPLVLL GQQLQQNMSL EPALEELLGL ADSLNSEDGV TGLELVDQAV
EVAPAPETTV AVNELEQTDN ADDFDDALVA ETLTIFIEEA EEHLSTIDQF LQTEDSKSQD
YNDLIRALHT LRGSSSMAQI DEIFEASSKV ENLFKTLLQE EIVSSSKEAA LLIQYAEFVR
DYLHVLRAGN TDNLQSIYAT FNKAWEDYGF ASQEHLESED NPQGLVSKLI ELNIDQLLDA
EFEFDKRALT EFPSYIETLS QQAQQLADHT NTRASVGIHD FTTELNAAYQ ALIQKPELLH
ADYAYELFAQ AHQEFIQLFD TLAAGQRVVL SEDIQKFLAE LTAYVQQDIE QFAKLKSADV
VDVAEAVEPV TQAEIHGVDD VQTSTSTAIK GVDFALLSQR VQQDHQQKQS DAANRDFDED
LLNIFIEEAE ELLVGIDQDL STWTRDQSNT AALNNLMRYL HTLKGGANMI SASHVGLIAH
ELESIYERII RQQISVSPSL IQIIRLVQDD IADRIQTIRE EAIDYPADQV IDILQNIQSI
STGEVSHVDV KAPAEQLDQP AAVVDDISVV EQFADNNTVD TEQVVDEPQL SASEIEIAQD
SAVEILEHAV AEHGQDVDDD LRAVMEETFL EESEEILEQA TQLLNHWIEQ RSDRNLLLQL
QRAAHSIKGG ARMVENEPVA SIAYQVETTF EQFAVHHFNS NAYDGLLKTT LSWLKQAIFN
KDYSNFDSIK LSLESIQYVD VTAQLPNLVA EIDQGIVTKG FEFIQGDGVE PPSMLGEWAE
ASNTDNSNEM IRISADLVEK MIDLSGENSI NRSRIEMDLG QLGNTLNEME LAIKRLADQL
RRMDGELESQ IIAKHGSENS RYADFDPLEM DQYSSINQLS KSLAESASDL VDFKSTLSEK
IRDAEGLLLQ QSRIQSEIQE SLMRTRLVPF DRLLPRLQRI VRQTSSTLNR PAELVVQNTE
GELDRTILER LVTPFEHMLR NAIDHGLEDT AERLALNKPE VGNIVLNISR QGTDVLVSFS
DDGKGIDEAK IKEKALKQGL IKADQFLDKQ EILQLIFHPG FSTAQAVTQI SGRGVGLDVV
QSEIKALGGH VSVDSEMGKG TTFTIRVPTT VAVSDALMVK AGDQQYAISL AQIERIVRIA
PSALEGYFNG KEDFFKIDNT NYKLRYLSEF VGNQPVPRLS NVAHSLPVLL IKGNSGQTIA
LLVDQLVGSR SQIVVKPIGQ QFTSVGAIAG ATILGDGQVC LILDGQNIAR QIQTTQRIKQ
SIDQRDLSRQ GNARRLVMIV DDSVTVRKVT SRLLERQGYD IVTAKDGVDA IEQLENVRPD
LMLLDIEMPR MDGFEVTNLV RHHDIHRDLP IIMITSRTGE KHRERAFSLG VTHYMGKPFQ
EAELLANIEA LIAEKQG
//
