ID M1P2L0_DESSD Unreviewed; 811 AA.
AC M1P2L0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Hemerythrin-like metal-binding domain-containing protein {ECO:0000313|EMBL:AGF77723.1};
GN OrderedLocusNames=UWK_01155 {ECO:0000313|EMBL:AGF77723.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF77723.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
CC -!- SIMILARITY: Belongs to the hemerythrin family.
CC {ECO:0000256|ARBA:ARBA00010587}.
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; CP003985; AGF77723.1; -; Genomic_DNA.
DR RefSeq; WP_015403417.1; NC_020304.1.
DR AlphaFoldDB; M1P2L0; -.
DR STRING; 1167006.UWK_01155; -.
DR KEGG; dsf:UWK_01155; -.
DR eggNOG; COG0840; Bacteria.
DR eggNOG; COG2703; Bacteria.
DR HOGENOM; CLU_347724_0_0_7; -.
DR OrthoDB; 9774644at2; -.
DR Proteomes; UP000011721; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd12107; Hemerythrin; 1.
DR Gene3D; 1.20.120.50; Hemerythrin-like; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000727; T_SNARE_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; PF01814; Hemerythrin; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00283; MA; 1.
DR SMART; SM00397; t_SNARE; 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; PS00550; HEMERYTHRINS; 1.
DR PROSITE; PS50192; T_SNARE; 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 Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000011721};
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 294..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 381..624
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 547..609
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT COILED 211..242
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 811 AA; 87620 MW; E2AC1266D2F4BAC5 CRC64;
MQNSMVKSFR FKLIAPIAIA LLVMIGSAII FTVLSQNSSS TQLNTKVVDS FETIQNTIGE
DLSKLSSQLD SNLKSMQTET SRTLAASSTE ALDNTATSVQ QSLRTIRRQS GNDLVQLMAL
VATNSVISKD FATLNSYVRS AHRNPDVLFI FYRDKDGTPL TRYINRANEK LKSLLPEGRP
DIAKIIQAGQ DDPNVLTLTQ EIKSNNDLAG SVSLAINMTQ AREEAEELKE EFNDLIAQNT
KQIDSILGRD SKAIGDELLQ VITQVKNKIT ENSGKTIADI TATSDSLSAR TRTLFTIGSI
VGFALLITIL FLNANSILKL LGGEPEAMVQ LARRIAGGDL SDQETGRSVP GSLQAALQDM
TVNLRNLIGN IVAEGRALTA TSTELALAAE DLTGGAEQSA AKADTVAAAT EEMSANMGTV
TMASEQAAQN VNVMANAMEE MSAAIQEIAE NTERANSMTG EAVNYAKSSS EKVNTLGAAA
REISKVTEVI TEISEQTNLL ALNATIEAAR AGEAGKGFAV VANEIKELAK QTAKATGEIK
NKIESIQSST DETVTEISEI SKVINSVNDI VSTIASAVEE QSVTASDISG NVNDAANGIS
EVNENVSQAS MVSGEIARDI VAVSQVSKEA REGSLRLQES AENLKEIADT ISRETNRFNL
GDTAGSHKQR QTVFTSGPLL RWSPSLALDI KSIDEQHKVL VNLINELHQK MNSNAPQNAV
GSVLGKLIDY TATHFKTEEE FFAQHRYEET DKHKEIHAKL VDQLLKFQKD YKAGEADISL
ELMEFLKDWL INHIKKTDAK YAPFLKSKGV V
//
