ID A0A0G4K317_9GAMM Unreviewed; 397 AA.
AC A0A0G4K317;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Methyl-accepting chemotaxis protein I (Serine chemoreceptor protein) {ECO:0000313|EMBL:CPR21407.1};
GN ORFNames=BN1221_04868c {ECO:0000313|EMBL:CPR21407.1};
OS Brenneria goodwinii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Brenneria.
OX NCBI_TaxID=1109412 {ECO:0000313|EMBL:CPR21407.1, ECO:0000313|Proteomes:UP000044377};
RN [1] {ECO:0000313|Proteomes:UP000044377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBR1 {ECO:0000313|Proteomes:UP000044377};
RA Paterson Steve;
RL Submitted (JAN-2015) 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}.
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DR EMBL; CGIG01000001; CPR21407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4K317; -.
DR STRING; 1109412.BN1221_04868c; -.
DR Proteomes; UP000044377; 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 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; 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; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|EMBL:CPR21407.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000044377};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 177..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 255..397
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 397 AA; 43566 MW; A48DD757C173E3F4 CRC64;
MAILLAIWGL ASGYSLYSLR QATDLLSKNE TQRKTYSYLV YGSDQYFRAV TRMERTMDYL
QHDDGDNAKK TLDMAQIAIK NSKESLENFK SSEHIGVEQA TLDEITHNWS TLISAAIDPM
NAALQQNNQD EFYRIFRGIY PPISLAFGDN VKAYTDQITA SEFIPVVNEY NIHNRNVLVA
AMIIGIMVLI FTEYYLRNYL VIPIGVLKSH LAQLTAGRLA GDLAEFGRNC AGRLIPDIKR
LQKSLRDTVT VIRQSATAID NGTANIKNGN DDLSSRTEQQ AAALQETAAS MEQISATVKQ
TAENVYQARE LAREAFGAAT KGGEISNSVM NTMDDISASS RKVADITTVI NGIAFQTNIL
ALNAAVEAAR AGEQGRGFAV VAGEVRTLAQ RAGGERD
//
