ID A0A0M2R879_9PROT Unreviewed; 510 AA.
AC A0A0M2R879;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=WH95_14645 {ECO:0000313|EMBL:KKJ76205.1};
OS Kiloniella litopenaei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Kiloniellaceae; Kiloniella.
OX NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ76205.1, ECO:0000313|Proteomes:UP000034491};
RN [1] {ECO:0000313|EMBL:KKJ76205.1, ECO:0000313|Proteomes:UP000034491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-1 {ECO:0000313|EMBL:KKJ76205.1,
RC ECO:0000313|Proteomes:UP000034491};
RA Shao Z., Wang L., Li X.;
RT "Genome sequence of Kiloniella sp. P1-1, isolated from the gut microflora
RT of Pacific white shrimp, Penaeus vannamei.";
RL Submitted (MAR-2015) 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 -!- SIMILARITY: Belongs to the short-chain fatty acyl-CoA assimilation
CC regulator (ScfR) family. {ECO:0000256|ARBA:ARBA00007227}.
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:KKJ76205.1}.
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DR EMBL; LANI01000021; KKJ76205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2R879; -.
DR STRING; 1549748.WH95_14645; -.
DR PATRIC; fig|1549748.8.peg.1680; -.
DR Proteomes; UP000034491; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; 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; cd00082; HisKA; 1.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR026281; HTH_RamB.
DR InterPro; IPR010359; IrrE_HExxH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR018653; ScfR_C.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF06114; Peptidase_M78; 1.
DR Pfam; PF09856; ScfRs; 1.
DR PIRSF; PIRSF019251; Rv0465c; 2.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000034491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 17..71
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 510 AA; 57042 MW; 2CE2EB150CBF9E9E CRC64;
MKAVNIMARQ VFAGRKIRHL RSQIGLTQLA MAKKIDISAA YLNLVEHNQR PLSRKLQKKL
EEAFNVKEGE LTGGEEARLL SAMNELFADP LFERSRPDTT VLGDFVAMHP EISRALLKLY
RAFRNAREDT LKARESISAD PYFTETSHQL LTQLTSIRSF AEILQDNDDL SEHQRERFTN
VLVDESQKLT SMVGELFDFI NGESKKGTLL SETPTDEVVD MLSANDHYFP VLEAAAEELR
GRLGEPKPYG LFDALAKYLD QQLGIQVEIV PVSSQGTLQR GMWELEGEDG GTLRLMETLA
TSSLNFRMAR IIAEVAYADV LEKVLADVPL SSDEAQSLCL KALGSYFAGA VMMPYSVFRI
AAYDLRHDID LLRRRFRAGF EQVCHRLTTL QKPEEEGVPF HFIRVDLAGQ ISKRFSASGL
RIPRYGVLSP DWGVQDAFLK PGRINLHSLR DEDQSVYFSI SKTVTKPGVM VGQAGNTYAV
SLGCEASFAR HVVYADGVDF SHPDSVLVGN
//
