ID B8FV44_DESHD Unreviewed; 577 AA.
AC B8FV44;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ACL18690.1};
GN OrderedLocusNames=Dhaf_0624 {ECO:0000313|EMBL:ACL18690.1};
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL18690.1, ECO:0000313|Proteomes:UP000007726};
RN [1] {ECO:0000313|EMBL:ACL18690.1, ECO:0000313|Proteomes:UP000007726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001336; ACL18690.1; -; Genomic_DNA.
DR RefSeq; WP_015942892.1; NC_011830.1.
DR AlphaFoldDB; B8FV44; -.
DR KEGG; dhd:Dhaf_0624; -.
DR HOGENOM; CLU_000445_107_27_9; -.
DR Proteomes; UP000007726; 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; 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 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 192..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..271
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 290..541
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 577 AA; 62166 MW; 25A52F36C48C6939 CRC64;
MGWFINLKTS RKLLICFLLM ALLILTVGIT GLLNLGKVNA NIKIITQDGI QPILILEDLN
KSFAKGAAEL TGVVWKSQVA EDSAVVGDSR RVIAQAIEDG DLLLQQYQML NLTDEEKELL
GEFKREEAVY RDLREKALTA VALKSYALAG DFNQQAGLQQ AKVEGIIDQM IECSLAYNEE
LQRASEQDFA KAGMVIMILT ACGFGLALLF SLLLGRMISR PILAAVEQAE LFAQGDFSTD
QQRAFLGRKD EIGQLAQAYD EIDSNMSRLL EQVMAAAEDL KTVGGELSVS AEELNAQGQN
INAGAEQIAA GMEETAASAQ EMLASGTEIS NGAGRLAGKA AEGSRIVQDI EQKAQLMRTN
AEASRGATLS MYQHKQAEII AAIQNGEVVQ EIRIMAETID GIAGQTNLLA LNAAIEAARA
GEQGRGFAVV AEEVRKLAEQ SAQTVAGIHA VISKVTEAFG QLSRNSSDVL TFMEEKVIPD
YESLVEAEEQ HAQDARRIGT LVEDFAATSE QMLAAIEQMS NAIQTVSASV QESTGSSQEI
AHNMSQMAGV MEQVAKAAQS QAEHAMDLNA MVEKFKI
//
