ID A0A2A2FC00_9GAMM Unreviewed; 2381 AA.
AC A0A2A2FC00;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 28-JAN-2026, entry version 32.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CK501_02730 {ECO:0000313|EMBL:PAU82083.1};
OS Halovibrio salipaludis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Oceanospirillales; Halomonadaceae; Halovibrio.
OX NCBI_TaxID=2032626 {ECO:0000313|EMBL:PAU82083.1, ECO:0000313|Proteomes:UP000218896};
RN [1] {ECO:0000313|EMBL:PAU82083.1, ECO:0000313|Proteomes:UP000218896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL5-2 {ECO:0000313|EMBL:PAU82083.1,
RC ECO:0000313|Proteomes:UP000218896};
RA Dong X., Zhang G.;
RT "Halovibrio sewagensis sp. nov., isolated from wastewater of high
RT salinity.";
RL Submitted (AUG-2017) 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:PAU82083.1}.
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DR EMBL; NSKD01000001; PAU82083.1; -; Genomic_DNA.
DR Proteomes; UP000218896; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 6.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 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; 8.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR051315; Bact_Chemotaxis_CheA.
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; IPR058661; FimL_2nd.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR003594; HATPase_dom.
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; PF26379; FimL_2nd; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 6.
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; 6.
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; 9.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 6.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PAU82083.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000218896};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 606..710
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 787..891
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 944..1047
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1291..1398
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1459..1562
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1590..1700
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1862..2095
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2097..2236
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 2259..2375
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 564..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..599
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..768
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..785
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..927
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1283
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1463
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1581
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1591
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1757
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 653
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 834
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 990
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1338
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1506
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1639
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2308
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2381 AA; 261467 MW; 8D24D6D8E3C77244 CRC64;
MATGVIMAQH DDSLSLHWVR GEIQETLRQS QHALEAFAEN REDLAQLRFC LNHLHQVHGT
LRMVQLEGAG LVAAEMEALA EALLNHEPGD SDTAIGSLMQ SILQLPDYLS TLQSRSEDVP
LRLLPLLNDL RAARGETFLS ASALFNPDLT PARFQAPAQV NQRLTASGVL DKVRKLQQMF
QFARAGLERG VDVDTHLDYL DKVITRLIKL CQRTPQGEIW QAAGALVDTL KSGHNAMGAA
TLALISDLDG ELERLISENE TILSQSVPED TLKNLLYYVA RGADCESERV STMVERYRLR
EALPDDTGDH GQSQAPARAA MSSVVEVLTE ELNTIKDRLD LFVRAHERSN ADLAELLPGL
RQVANTLAML RQGTSQRVIN DQIERIDQLA ASADAVDDGT LMDIAGALLY VEAAISGLSE
GESQQTSDAG DSTDHRITGI QATEAGGAVL RESRNALEQV KTGVVNFIAS QWNTDAISGV
PELLYSIRGS LHLIPLERTA TALGACERFI QDVLIDGVWT PNWEQLDTLA DAITSIEYHL
ERLMDGIDDN DAILAMAEER LESLGFPPGR EPTRTAPEQE ADEATEAAPA DSAAAATAEP
PKERDSELLD DDILEIFVEE ADEVLEAIQQ HYPTFRADHE NHQALSEVRR AFHTLKGSGR
LVGATSIGEL AWSVENLLNR VLDRSIQPGE RIMSLLDRVI ERLPGLIQSF RDGEATGDVD
DLMSEAHGLA DTRNAEEPED TDAEHAVREE PEPEPEPEQE DRETEAEPQP ETTAAPVPET
EASAADEPLV DQEILDIFIE EAEEVLETIH EYLPRLLESY ENTSALTEVR RAFHTLKGSG
RMVEAERIGE LAWAVENALN RVLDGTLFMS DDMASVLQEV TNAIPTLVED FRQQRAPSVD
TTRLEERANA LARGEVLDAE PMPEAEPEAP APEAPAEELA DVEEPELDPM LMDIFRSEAD
SHLEALDTFL ADAEGQETAD YTDNLSRALH TLKGSAHTAG IEPIARVTAP MEKFVKRARA
AGDRADPEVI SLIRRVRDFV QEGLERLTSD PLTPLDGTDT FLTDLRNLHQ ARYPDEAPPA
GTTTPETGTA GDNSLISIFL NEGIEQLLDA DQTLEQWLEG NTGEAPLKAL IDSLATLSAS
ADRAQVQHVS ELAGALQHLY EEVIETTDLP VDQLTPLLRE AHEAMINLMD QLAAGLATES
PAGLVTRLNE QAADLRQART DAEQQVFEER FGGDLASMDE ALNEDIEAEP APEPEPEPEP
EPEPEPEPEP EPEPEPEPVE QDETASGGEA SADIDPELAE IFLEEAHELI DSTGEALHQY
ISEPDNTELA KTLQRELHTL KGGARMAEIA PIADLSHSLE DLFERVAEGR LALGEATGDT
LLACHDALAR MVDQTSAFQP CEPADELTER VHALMRGETA TPAAETEAKE PEPEPEPEPE
TSEQTSTAEA TAEPEAEPTS APENELSVLF LDEAREIENA LEQAVRDWEG DPEQGEPMAR
MREELHTLKG GARLSELEPI AELADTWEST LDSVIEGAGD SHQALSFSQQ SLTRLGGMLD
RVEAGESLAA DATGAEAGET TTGDEAEDDP SNVDPEVLEI FLEEAGELVD TLDHTLAAWQ
KAEDGDEATH SQEAQRALHT IKGGARLAEL TTLGEKAHRF ESLLSRIESE GNRPTEDQWE
EIHGLHDEII SRVEQVRRTW QGDAGEQQPE AAAPAPQTEP AGAGETTGAP EEPAEPEAQN
TPETTAGEQQ TQPQQQARDQ RRAELARSAQ ETLRVNAQLM DEMVNLAGET SITRGRLEQQ
ISDFSHTLDE MAATTDRLRE QLRRMEIETE AQILHRAEQE FGPDYDQDFD PLEMDRYSAI
QQLSRALSES ASDLADLRET MSDKVRDAET LLLQQQRTNT ELQEGLMKTR MVPFSSMVPR
LRRIVRQISG ETGKKAHFEV NNAEGELDRT VLDRMVAPLE HMLRNAIDHG IEDAGEREQA
GKPTTGNVRL DLSREGGEVV LRLRDDGGGI DTEKVRQKAI KQGLLESGED LTDHEILQFI
LQPGFSTAAS VTQISGRGVG MDVVASEIKQ LGGSLDINST LGEGTIFTVR LPFTVSVNRA
LMVTIGDDYY AIPLNTIEGI VRVSTYELEE YYQPDAPMYE YAGQQYRLQY LGALLNSDSQ
PKLQGQALPL PVMLVRGADQ PMALQVDSLM GSREIVVKSL GPQFGSVRGV SGATILGDGN
VVVILDLPAM IRGDILAQRQ RMLAQVETRE TPREQRPTQV MVVDDSVTVR KVTSRLLERH
GMEVLLAKDG LDAVGQLQDR RPDIVLLDIE MPRMDGFEVA SFIRHDSKLS DVPIIMITSR
TGDKHRERAE AIGVNHYLGK PFQEQELLDT IMEHASVGEE Q
//
