ID A0A0F5ATB2_9GAMM Unreviewed; 771 AA.
AC A0A0F5ATB2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=WN56_00710 {ECO:0000313|EMBL:KKA45691.1};
OS Salinivibrio sp. KP-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Salinivibrio.
OX NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA45691.1, ECO:0000313|Proteomes:UP000033449};
RN [1] {ECO:0000313|EMBL:KKA45691.1, ECO:0000313|Proteomes:UP000033449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KP-1 {ECO:0000313|EMBL:KKA45691.1,
RC ECO:0000313|Proteomes:UP000033449};
RA Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA Kaur N., Bala M., Mayilraj S.;
RT "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT nov., a novel halotolerant gammaproteobacterium isolated from marine
RT sediment and emended description of the genus Salinivibrio.";
RL Submitted (MAR-2015) 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:KKA45691.1}.
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DR EMBL; LAQR01000001; KKA45691.1; -; Genomic_DNA.
DR RefSeq; WP_046073149.1; NZ_LAQR01000001.1.
DR AlphaFoldDB; A0A0F5ATB2; -.
DR PATRIC; fig|1406902.3.peg.150; -.
DR OrthoDB; 9806704at2; -.
DR Proteomes; UP000033449; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd11386; MCP_signal; 1.
DR CDD; cd18774; PDC2_HK_sensor; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR32089:SF120; METHYL-ACCEPTING CHEMOTAXIS PROTEIN HLYB; 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 PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50192; T_SNARE; 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, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000033449};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 416..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 440..493
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 498..734
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 685..747
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 547..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 83982 MW; 18E61D5A070D8303 CRC64;
MRISNKITLA IVAASLTCVL TIAAILAFRT IGLSSQALDK KVKSQLTAVK ASKKSEISNY
FKFIGDQINT LSDSTMTEDA LAQLAQAFNT IAADTANSPS QESQLASYYR NQFGATYQEI
NDTSTDVMGR YNQLPDVAKR LQHAYISGNP HPLGSKDAMA KANDGSVYSE IHSVFHPNFQ
HYLKTFGYYD IFLVDNQGNI VYSVYKELDY ATNLLTGPYS TSGLADAYKA VRKAPQGELG
FIDFRPYYPS YDSPASFISS PVYKNGQQIG ALIFQMPIDR ISELISNNGQ WAESGMGTSG
EILLVGPDNL LRTQPRLLSD DKDAYLSALE SQGLNADTIH RIDYQNSAAG NQPLDNPAVK
RALRGEQGFV TQTSYRNTEV LASYSPIDVY GVTWAVISQQ DTDEVFTAIT KLRTDIGVVT
AFTAVLLGSL AALAAYWLGK SIGAPILKLA TNIKQVADSK DLTITLHHTS KDELSTLADS
LNEMFQSFRD VIQKTHDASK TLLSSANDIS DDVVAVRGQV DEQAKSSNQV ATAATQMAAS
ISEVSEHASN ASEASDTITQ TANEGSQKGE ALVSQMQTLK DHMDKATRSM EKLSHESESI
GSVLDVIQEI AEQTNLLALN AAIEAARAGE QGRGFAVVAD EVRSLATRTQ SSTEEIRAKV
DALQQETRGA ADGMTQANDA VTQSVEHCHE NNDKLGQIKT MIEQINEMNM QIATAANQQT
QVTDEISQNV NTMAQSADHV SERTRNTEQT VNHLREHART LEARISHFKT D
//
