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Database: UniProt
Entry: K0CKU3_ALCDB
LinkDB: K0CKU3_ALCDB
Original site: K0CKU3_ALCDB 
ID   K0CKU3_ALCDB            Unreviewed;       537 AA.
AC   K0CKU3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Chemotaxis sensory transducer {ECO:0000313|EMBL:AFT72362.1};
GN   OrderedLocusNames=B5T_04102 {ECO:0000313|EMBL:AFT72362.1};
OS   Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS   B-5) (Alloalcanivorax dieselolei).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alloalcanivorax.
OX   NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT72362.1, ECO:0000313|Proteomes:UP000006286};
RN   [1] {ECO:0000313|EMBL:AFT72362.1, ECO:0000313|Proteomes:UP000006286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC   {ECO:0000313|Proteomes:UP000006286};
RX   PubMed=23144414; DOI=10.1128/JB.01813-12;
RA   Lai Q., Li W., Shao Z.;
RT   "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL   J. Bacteriol. 194:6674-6674(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003466; AFT72362.1; -; Genomic_DNA.
DR   RefSeq; WP_014996413.1; NC_018691.1.
DR   AlphaFoldDB; K0CKU3; -.
DR   STRING; 930169.B5T_04102; -.
DR   KEGG; adi:B5T_04102; -.
DR   PATRIC; fig|930169.3.peg.4064; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_16_6; -.
DR   OrthoDB; 2489132at2; -.
DR   Proteomes; UP000006286; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProt.
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; IPR004089; MCPsignal_dom.
DR   InterPro; IPR033480; sCache_2.
DR   PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF17200; sCache_2; 1.
DR   SMART; SM01049; Cache_2; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006286};
KW   Transducer {ECO:0000256|PROSITE-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        189..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          268..497
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          513..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  58700 MW;  E9421D6AE1543B8C CRC64;
     MKQWTMTRQL WGMLGLLWLA MLLLAGWTAW DNRQTILTER KTGLSQYVDS ALNAVDGQAR
     LAASGVISET EARQRAEELI RDMTYDEGRG YLYAFDENHR MLTHPSLAKG TNMWDYQNEE
     GRYLFREFME AVQNGDGFVD YLWVHPGQEG LAKKSSLHVH YPLWDWYLGS GVYINDINDA
     FYASLTQSLL FLLALGIPLT LLMGVIIRGV LRRLGGEPGY AAEAVRYISE GDLSQPTRLK
     DGDTGSLLFD IERMRQSLGA TVGDIHRSAD VVNTAVEDIK AGNDELATRT EQQAASLTET
     AASMEQLTTT VQQNADHAEQ ARHLANSTAG DARRGSDAMD TVIHTMGSIH DSAEQMSAIV
     DAIDEIAFQT NILALNASVE AARAGEQGRG FAVVAEEVRN LASRSAEAAG EIKTLIESAG
     TLVATGSQQV RGTGEIITGM VADIGRLSTL VSEIATASNE QSQGIGQANE AITQMDMMTQ
     QNARLVQESF SAAQRLVDQS QQLRLYVARF QVKPPPRTGT ADDHDLLQSE KAVPAPA
//
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