ID A0A0M2R6K2_9PROT Unreviewed; 423 AA.
AC A0A0M2R6K2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KKJ75133.1};
DE Flags: Fragment;
GN ORFNames=WH95_20040 {ECO:0000313|EMBL:KKJ75133.1};
OS Kiloniella litopenaei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Kiloniellaceae; Kiloniella.
OX NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ75133.1, ECO:0000313|Proteomes:UP000034491};
RN [1] {ECO:0000313|EMBL:KKJ75133.1, ECO:0000313|Proteomes:UP000034491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-1 {ECO:0000313|EMBL:KKJ75133.1,
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 -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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:KKJ75133.1}.
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DR EMBL; LANI01000052; KKJ75133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2R6K2; -.
DR STRING; 1549748.WH95_20040; -.
DR PATRIC; fig|1549748.8.peg.3974; -.
DR Proteomes; UP000034491; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000034491};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284}.
FT DOMAIN 117..169
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 174..403
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 180..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 374..412
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKJ75133.1"
FT NON_TER 423
FT /evidence="ECO:0000313|EMBL:KKJ75133.1"
SQ SEQUENCE 423 AA; 44856 MW; 0E542EDAAB2DAB0D CRC64;
LVGFDTNKLL GGSIDRFHKN PAHQRTMLEA LTTTYQGRIN VGGRTFDLIA NPITNQDGER
LGTVVEWADI TAELAIEAEV DQMVNAISKG DFTKSLSAEG KEGFMLALTN ALNSLNKNVS
DVIDDVATAL SSLSRGDLTH EITTDYTGMY ETLKQDVNQT SKRLSETVGE IITTTDEIGS
ASTEISSGSM DLSQRTEAQA SSLQQTAASM EEMSTTVKQN ADSAQQANQM ALNATETAER
GGEVVQEAVV AVTGIEQASQ KVSDIIGVID EIAFQTNLLA LNAAVEAARA GEAGKGFAVV
AAEVRTLAQR SGEAAKDIKT LIMEANDQVK EGVTLVRSTG DTLSEIVDSS KRVADIISEI
AASSREQASG VEEINAAVTA MDEMTQQNAA LVEESSAAAR TLEEQAEGLS EMIGFFKTNN
TGR
//