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Database: UniProt
Entry: A5MZG7_CLOK5
LinkDB: A5MZG7_CLOK5
Original site: A5MZG7_CLOK5 
ID   A5MZG7_CLOK5            Unreviewed;       571 AA.
AC   A5MZG7;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Predicted methyl-accepting chemotaxis protein {ECO:0000313|EMBL:EDK34263.1};
GN   OrderedLocusNames=CKL_2251 {ECO:0000313|EMBL:EDK34263.1};
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK34263.1, ECO:0000313|Proteomes:UP000002411};
RN   [1] {ECO:0000313|EMBL:EDK34263.1, ECO:0000313|Proteomes:UP000002411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC   {ECO:0000313|Proteomes:UP000002411};
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000673; EDK34263.1; -; Genomic_DNA.
DR   RefSeq; WP_012102593.1; NC_009706.1.
DR   AlphaFoldDB; A5MZG7; -.
DR   STRING; 431943.CKL_2251; -.
DR   KEGG; ckl:CKL_2251; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_27_9; -.
DR   Proteomes; UP000002411; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF12729; 4HB_MCP_1; 1.
DR   Pfam; PF00015; MCPsignal; 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:UP000002411};
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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          212..264
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          283..534
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   571 AA;  62671 MW;  2BF13CFF044A79A1 CRC64;
     MKKFNNLRIR SKLLVSFLSI VLFIVIIALI SMINMGKINT GSNQLYSNNL RTLRNLDKFD
     ANTLHLRLSI INLVESRDNS KVSDTITSMD NLKSENNSIL NEYKKGNLTN QEKDILVRLE
     SELTDWRNIC NDIVKLMADD KYDDAMALNK EAASYRDKLT KSIEQLVEIV DKKAKDSNME
     NTSLYNTSLY IIILIVAAAL IISLVVSFKI SSSISSQVFK ILSFTELISK GDLSETINSS
     SKDEIGLIAE KLNDANESIK GLVGEILHGT EDMSASSEEL SATAQEISSM MISVNEATDH
     IAKGAQNLSS ITENISQSSE EMESSISELS NKAEESAKSS LEIKKRAANI KETASKNIEE
     GENIYNDKKG NIIKAIEDGK VVSEVKIMAA SISSIAEQTN LLALNAAIEA ARAGEHGRGF
     AVVADEVRKL AEQSSSTIDT INKMVFSVET AFKNLSKSGE EILDYIANNV KPSYEFLMNT
     GVQYEKDAEF ISNISQEIDS ASKHMKQLVS KVNDAIQGVA STAEESSSES QEISSSINEV
     TKAIEDISAS SESQAELAEK LTHIVNKFKV N
//
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