ID A0A1C0A928_9FIRM Unreviewed; 529 AA.
AC A0A1C0A928;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=U472_10145 {ECO:0000313|EMBL:OCL26745.1};
OS Orenia metallireducens.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Orenia.
OX NCBI_TaxID=1413210 {ECO:0000313|EMBL:OCL26745.1, ECO:0000313|Proteomes:UP000093514};
RN [1] {ECO:0000313|Proteomes:UP000093514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z6 {ECO:0000313|Proteomes:UP000093514};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OCL26745.1, ECO:0000313|Proteomes:UP000093514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z6 {ECO:0000313|EMBL:OCL26745.1,
RC ECO:0000313|Proteomes:UP000093514};
RA Maxim B.I., Kenneth K., Flynn T.M., Oloughlin E.J., Locke R.A., Weber J.R.,
RA Egan S.M., Mackie R.I., Cann I.K.;
RT "Orenia metallireducens sp. nov. strain Z6, a Novel Metal-reducing
RT Firmicute from the Deep Subsurface.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the hemerythrin family.
CC {ECO:0000256|ARBA:ARBA00010587}.
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:OCL26745.1}.
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DR EMBL; LWDV01000009; OCL26745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C0A928; -.
DR Proteomes; UP000093514; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd12107; Hemerythrin; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.20.120.50; Hemerythrin-like; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
DR InterPro; IPR004089; MCPsignal_dom.
DR NCBIfam; NF033749; bact_hemeryth; 1.
DR NCBIfam; TIGR02481; hemeryth_dom; 1.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF01814; Hemerythrin; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF47188; Hemerythrin-like; 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}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000093514};
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 9..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..126
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 124..360
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 268..306
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 352..386
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 529 AA; 59558 MW; 69A7A43CB8C4A9CD CRC64;
MNLKIKHKIL LSITLGLIVA LLSVGIVVNL QFNNFVEKQN VNLEDLKIEI LTAIGVTFII
ISLLITFIML RLSNYISKGL AKITYGMKQL ATGDLTIRLE VNKQDEFGQL YQSFNESVKE
QSILVNKILE DAESLLLYSE ILSASTEEGN AAIETTNQLI ESMSANIQEI SASGEEVTSF
AEESTAQTQS GKENMVETVS RMEEINQKVK VTVDLIKELN SNSEEIGGII ELITNVADQT
NLLALNAAIE AARAGEHGQG FTVVAEEIRE LAEETTKATV NVKRLIENTR INSQNVIKAI
KEVEEKTLEG QTITESTNQI FAQIEEASEE TTAQIEQIAY GAQDLANDSE ALVLAAKDID
NMSQEINNSS NELKDKANDL KSLVAKFVLE DKVAVTKWND KYKVGVEKID EQHKGIFERA
NYLLDAHKNQ SSEKDIEEVM DFLANYIDKH FREEEEIQRK YEYPDYENHK KIHHNFESKV
KEVIADYKNS TVKVTSLMKL NKMVTGWLIE HIKREDQKLA EYINNSQIS
//
