ID A0A261VXP8_9BORD Unreviewed; 502 AA.
AC A0A261VXP8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:OZI78063.1};
DE Flags: Fragment;
GN ORFNames=CAL24_10210 {ECO:0000313|EMBL:OZI78063.1};
OS Bordetella genomosp. 2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1983456 {ECO:0000313|EMBL:OZI78063.1, ECO:0000313|Proteomes:UP000215633};
RN [1] {ECO:0000313|EMBL:OZI78063.1, ECO:0000313|Proteomes:UP000215633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU8256 {ECO:0000313|EMBL:OZI78063.1,
RC ECO:0000313|Proteomes:UP000215633};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZI78063.1}.
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DR EMBL; NEVT01000005; OZI78063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261VXP8; -.
DR Proteomes; UP000215633; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR035440; 4HB_MCP_dom_sf.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 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 Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..265
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 270..499
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 289..323
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 502
FT /evidence="ECO:0000313|EMBL:OZI78063.1"
SQ SEQUENCE 502 AA; 53553 MW; 751E12D60E291E20 CRC64;
MLSNLKVRTG MALVLGAFLL ALLFSNAAGW LAMYSSNDKL DRVNSVYSYQ AVPVYSAYTL
LQRSRLDLAA AMIEMQEGRS RESGQFLGRA RDRDEAASQT MAAFMKIERQ GELADKAAAV
QAAYQGYAGQ SRRQMDALAR QDVRGFIGLN AALQTQGARF DEAVNAYLAY VDTRTNDLVA
QADADYTLSQ RVSAVMVALS LVLAVVCWAF MQRGVLRPLR HAGQHFDKIA AGDLTARVEV
RNNNEIGQLM AALKRMQENL ARTVSQVRRG VDEINVGARE ISAGNTDLSS RTEQQAASLE
ETAASMEELA STVKQNADNA RQANQLAASA SDVAERGGAA VSEVVSTMED ISASSRKISE
IVSVIDGIAF QTNILALNAA VEAARAGEQG KGFAVVAGEV RSLAQRSAQA AKEIKVLIED
SVSKVGTGSQ QVERAGATMQ EIVASVKRVT DIMGEISAAS EEQSGGIDQV NRAVSQMDEV
TQQNAALVEE AAAAAGSLQE QA
//
