ID A0A1D8GHH8_9CLOT Unreviewed; 570 AA.
AC A0A1D8GHH8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Gferi_12675 {ECO:0000313|EMBL:AOT70371.1};
OS Geosporobacter ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Geosporobacter.
OX NCBI_TaxID=1424294 {ECO:0000313|EMBL:AOT70371.1, ECO:0000313|Proteomes:UP000095743};
RN [1] {ECO:0000313|EMBL:AOT70371.1, ECO:0000313|Proteomes:UP000095743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRF9 {ECO:0000313|EMBL:AOT70371.1,
RC ECO:0000313|Proteomes:UP000095743};
RA Kim S.-J.;
RT "Genomic analysis reveals versatility of anaerobic energy metabolism of
RT Geosporobacter ferrireducens IRF9 of phylum Firmicutes.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP017269; AOT70371.1; -; Genomic_DNA.
DR RefSeq; WP_069977050.1; NZ_VENK01000005.1.
DR AlphaFoldDB; A0A1D8GHH8; -.
DR STRING; 1424294.Gferi_12675; -.
DR KEGG; gfe:Gferi_12675; -.
DR OrthoDB; 1887545at2; -.
DR Proteomes; UP000095743; 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 Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000095743};
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 13..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..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..541
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 152..183
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 570 AA; 63229 MW; B4BD11D9225E707B CRC64;
MKWLSNLKIG TKLISAFLIG ILLMGSLGWI GIKSLKDTDA RIESMYTDRV IPLEQISDVQ
KNVLSVRLNL SFLMMPNNTL SVSEVEKLVT LARNSNDELM KSYTDTYMTE EEKLMIESFN
SKLASYRMAQ DKYLRFIKEN KMDEAMVEFD NLTIWENSIQ QALQQLVDLN KQLMEDVMKE
NKKAYAKTVQ DTLIYLAIAI VFALSMGIIL TKIITNGLRK VIEFAEGFGN GDLTRQMDVH
TEDEIGTLVR ALNRAVQNTQ NLIKEIVNNA AHMNTSSQEL SATIEEVLAQ AHNIDAATQG
ISKGTEDTSA SLEEVNASGQ EVAAAVNRLA VRAKEGNFES IEISKRAEGM KESAEQSRQV
AQDIYKEKQR SILQAIEAGK VVGEIETMAT AISAISDQVN LLALNAAIEA ARAGEHGRGF
AVVADEVRKL AEESSKAVSN IQETIKHVYG AFNNLSRNSN DILQFIDEKV HKDYETLVDT
GIQYKKDAEY MNRLIFEFDQ NAQSIAEAVN QINVAIESVS ATSEQTTAGT QEISSNVSEV
ADALEEVAKV SQKQAELAGT LNHMIQKFKI
//
