ID A0A0F7JVZ6_9GAMM Unreviewed; 542 AA.
AC A0A0F7JVZ6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AAY24_04700 {ECO:0000313|EMBL:AKH19772.1};
OS Sedimenticola thiotaurini.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH19772.1, ECO:0000313|Proteomes:UP000034410};
RN [1] {ECO:0000313|EMBL:AKH19772.1, ECO:0000313|Proteomes:UP000034410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH19772.1,
RC ECO:0000313|Proteomes:UP000034410};
RX PubMed=26089430;
RA Flood B.E., Jones D.S., Bailey J.V.;
RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL Genome Announc. 3:e00671-15(2015).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP011412; AKH19772.1; -; Genomic_DNA.
DR RefSeq; WP_046858708.1; NZ_CP011412.1.
DR AlphaFoldDB; A0A0F7JVZ6; -.
DR KEGG; seds:AAY24_04700; -.
DR PATRIC; fig|1543721.4.peg.986; -.
DR OrthoDB; 2489132at2; -.
DR Proteomes; UP000034410; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 3.30.450.290; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000034410};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..265
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 270..506
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 310..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 59003 MW; 309B7BAB8420442C CRC64;
MKKASNNRAS GLSISTKIDL ALVVLFLIIL IVSALYQFNS QRDLVEHMVM DQTETLADSY
FDNVNTLMLT GGMANKEIPR KKVIAREDVL DARIIRGKAI IDTYGAGTEQ NEIRDDLDKR
ALAGEKIDEL YRDENGRVLT VILPMFAKKD YRGTNCLLCH PVPENEVLGA VRVDYSLKIL
DDKVLKELWT NIGLNSALLI GGLIIISFIL KKLVVARLRR VTELVRTIER ESDLGLRASD
HSSDELGRLA QAINLMMEKF SSIINHVNNS TQQLAEESTH LTDITTQSIE GVRRQQMESQ
QVATAMTEME ANSNEVASSA ANASDAANHA DTEAAEGGKV VSSAIASINA LASEVNQAFD
VIRQLEADSD GIGKVVEVIT NIAEQTNLLA LNAAIEAARA GEQGRGFAVV ADEVRTLATR
THQATQEIQG MIEGLQQQSQ NAANMMSQSQ QRVEATVAEA GHVGESLNKI THSINTISQM
NEHIATAAQQ QSMVAGEISR NITAISDVTG QTADHSEQIA QTSKQLAGLA SELREEMAQF
KV
//
