ID A0A091B4T7_9GAMM Unreviewed; 1181 AA.
AC A0A091B4T7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=HPt domain-containing protein {ECO:0000259|PROSITE:PS50894};
DE Flags: Fragment;
GN ORFNames=N790_07665 {ECO:0000313|EMBL:KFN47633.1};
OS Arenimonas malthae CC-JY-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1384054 {ECO:0000313|EMBL:KFN47633.1, ECO:0000313|Proteomes:UP000029392};
RN [1] {ECO:0000313|EMBL:KFN47633.1, ECO:0000313|Proteomes:UP000029392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-JY-1 {ECO:0000313|EMBL:KFN47633.1,
RC ECO:0000313|Proteomes:UP000029392};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas malthae.";
RL Submitted (SEP-2013) 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:KFN47633.1}.
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DR EMBL; AVCH01000160; KFN47633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091B4T7; -.
DR STRING; 1384054.N790_07665; -.
DR eggNOG; COG2198; Bacteria.
DR Proteomes; UP000029392; Unassembled WGS sequence.
DR GO; GO:0004672; F:protein kinase activity; IEA:UniProt.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.20.120.160; HPT domain; 3.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01627; Hpt; 3.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 4.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 699..806
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 580..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1108..1179
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 591..608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 746
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT NON_TER 1181
FT /evidence="ECO:0000313|EMBL:KFN47633.1"
SQ SEQUENCE 1181 AA; 124361 MW; B16124284490144C CRC64;
MRLHENIDFT TLTWVKPELD ETLRQARLAL ETYVEDGEDP GQLKACANLL HQVQGTLRMV
ELYGAAMVAE EMEQLAKALV EGKVAERESG YAALMRGIVQ LPDYLERLQS GHRDIPIVLL
PLLNELREPR GEKGLSESVL FSPDLSRPLP ASAAGPAAPL APEELKRRAE TLRGLFQSAL
LRWLKDDNSA ANIRDLTDVC EQLVPITDAE HARRLFWVAA GTLDALARNA FEAGKPLKQA
LAKVEQEIKR LAEGGDAAFR SDPPLELTRQ LLYFVAHAPT DNGRIGEIRE VFGLGQYLPS
ESELAHARGS LSGRNKALLS TVAAAIKEDL LRVKDALDLH LRSPEAPAAE LGEQAEALDR
VADTLGMLGL GVPRRVVQDQ RTAIHAISSG ERKADESSLL DIAGALLYVE ASLDDQVARL
GEAEVGPEAE AAAAAERALP SSEARMVLEV LVKEAIANFA QARQCFVAFV ETHWDHAQLA
DVPRLLEEVA GALRILEVQD APQYLAAVRR FTESELLRRR RVPNGQQMDR LADALAGLEY
YLEALRDRRP KREQILDIAR QNLESLGYWP LPAEDLAPPS AAVPTAAAEP VAPAPAAPAP
EPVVEAPPAP EAEPVAEAAA EPALDFSDFS LDLGQPPEIE LPAEIAAPGV SFEPIVEPQP
EPVAEMPPVA GPPVPQPEPV AAAPAVSGPP AIPGFDGTSD EIDDEIREVF LEEFQEEIGN
LEQLLPNWRK QPDNMEQLRP IRRVFHTLKG SGRLVGAKTL GEFSWKVESM LNRVLDGTRP
ASPAVVSLIE HAFNTLPLLR AALQGETVHA DLAGIESLAE RVAAGEEAFY QPPSAPAAEA
VAPAPAPVAE VAVPAVPAEP EPVLPEVVSP AIEMAEAAAD SGFAIDPVLF EILKPEVAGH
LETVDAWLAT AAGGMQPVTD PLLRAVHTMN GAFAMTEVTA LTEVTAPLEG FLKRSLAAAR
PPSAEGVAVI GEVAAAIRQV IAALELPRPN LPSYAALAAR VVALRDALPE STSPSMPMHP
EDVESVMPTA VSLGAPDLSG LPSFEVETPE PAASLASPEA DLPADEPAQE VVSLDAFLDT
GLGEAEAPLS LSVTEATVED AVSAEEIAAA EAALLAAAEA EAAAAEAAAA AAAAEAAAAE
AAAAEAAAAE AAAAEAAAAE AAAAEAAAAE AAAAEAAAAE A
//