ID A0A1C0YCX6_9BACL Unreviewed; 652 AA.
AC A0A1C0YCX6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A6M13_14160 {ECO:0000313|EMBL:OCS85022.1};
OS Caryophanon tenue.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Caryophanon.
OX NCBI_TaxID=33978 {ECO:0000313|EMBL:OCS85022.1, ECO:0000313|Proteomes:UP000093199};
RN [1] {ECO:0000313|EMBL:OCS85022.1, ECO:0000313|Proteomes:UP000093199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14152 {ECO:0000313|EMBL:OCS85022.1,
RC ECO:0000313|Proteomes:UP000093199};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Caryophanon tenue genome sequencing.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OCS85022.1}.
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DR EMBL; MASJ01000017; OCS85022.1; -; Genomic_DNA.
DR RefSeq; WP_066545252.1; NZ_MASJ01000017.1.
DR AlphaFoldDB; A0A1C0YCX6; -.
DR STRING; 33978.A6M13_14160; -.
DR OrthoDB; 9762005at2; -.
DR Proteomes; UP000093199; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000093199};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 295..347
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 366..637
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 652 AA; 71940 MW; BCFB3F32382F6FB7 CRC64;
MKKKSIRTKL IGLLVVALTI IMTFSSVMII NLFKEEIETM LQEETVEKVA FLNTFLDNYL
ETPIALVEHT ATHVIVPANE EEKAILHTQL QAKAEGIQGV LGLHVAYDGD PLLYSSEALT
LASDYDANTR EWYIEAKENP TEILVTDPYV DAITGKLIVG VSKMMSNGQG VVTLDLDLAF
LENIASTIIV GDTGYTFVFD QNGKVLYHPN FEQGELVTDV PFYEAFMETN YLETEDEGTH
IYINRFFNET MNWQIGSIYT ESDIDSAYKD SVSSIVAINT ICIVVLLMIF FVIVTRIIRP
LKQVMAHAQD VAQGDLTKQV MIQTTDEIGQ LSASFNGMTT SLQTMVRSVD ETSTRLHHFT
TDVSSSVEEN VQSIHQVVGH IQAVSEQSKD QLVATQDVQH IVQHMGQQVD QIAQNVNEVR
TASAKAEQET LSGVEMVTAV RQQMQQIATY AQETAINFNE LITVANHIQS FSEGISGIAA
QTNLLALNAS IEAARAGEHG KSFAVVAEEV RKLAEQTNTS ASEIQTLVAT IQKTGAVAND
SMKESGDAVQ DGLEKIADAH ERFIVIQHVM LTLATRVNEA ETMLAQLNDS KETAIEAVSH
ITETTKEVSQ NIEHVAATTE EQNMSMEQMA IAAEQLAQQA QQLQALIRRF TV
//
