ID A0A160JH17_9PROT Unreviewed; 726 AA.
AC A0A160JH17;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ANC92276.1};
GN ORFNames=A6A40_10380 {ECO:0000313|EMBL:ANC92276.1};
OS Azospirillum humicireducens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC92276.1, ECO:0000313|Proteomes:UP000077405};
RN [1] {ECO:0000313|EMBL:ANC92276.1, ECO:0000313|Proteomes:UP000077405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC92276.1,
RC ECO:0000313|Proteomes:UP000077405};
RX PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium isolated
RT from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP015285; ANC92276.1; -; Genomic_DNA.
DR RefSeq; WP_063635341.1; NZ_CP015285.1.
DR AlphaFoldDB; A0A160JH17; -.
DR STRING; 1226968.A6A40_10380; -.
DR KEGG; ahu:A6A40_10380; -.
DR OrthoDB; 9814362at2; -.
DR Proteomes; UP000077405; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd12913; PDC1_MCP_like; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
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.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 380..432
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 470..692
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 622..684
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
SQ SEQUENCE 726 AA; 76501 MW; 8D392C3B6EAF5AF4 CRC64;
MQTKSIQSKI ALLAGMCLAG TVAVLVGFGI VSTRSNDEFV TDNVERILES KTTESLQNLA
ATQAGLLRSE FDSALNAART MAGSFASLAD DASPGHILPE RRREVLNGVL LSVLKQNPLF
NGTYSAWEPN ALDGRDEEFR NRRETGTDGT GRFIPYWNRD QNGRIAMQPL VEYDSRDRHP
NGVMKGGWYI GPQEHGRESV LDPLPYIVQG KQVFLATLSV PVVIGGKFRG VAGADFNLDF
VQQLSTKVSA AVFDGRSQVV IVSNMGLIVA HSARPDLIGQ PISTFDTSWQ SDLANVQAGK
AHVDIEATTN MLRAFAPITL GNTEKPWAVL VQVPKDLVLA HSMALSEALG ERANSNILWQ
VAVGALVALC AVAVMWVVAG GIARPIRASV GFAEGIAAGR FDQTLDIRQS DEVGALADAL
RKMLADLKRM IDQRAEDQAK ADAERRTAML QLADTLEAQV MNVVDGVDRA AQSMTGTAQS
MTATATQTSQ QAGVVASASQ DASSNVQTVA SATEELSASI QEIGERVNRS AQIAREAVEA
AQQANGQVLS LTEAAEKIGT VVQLIQDIAS QTNLLALNAT IEAARAGEAG KGFAVVAQEV
KSLASQTAKA TEDIAGHVSG MQRVTNETAN AIKGIGGIIA QIDEISTAIA AAVEEQGSAT
AEIARNVQQA ASGTQEVTKT IADVRSAAVE AGHSAENVLS VSGQLAGDAG RLRSAVNGFL
STIRAA
//