ID A0A964BTG3_9CYAN Unreviewed; 752 AA.
AC A0A964BTG3;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE SubName: Full=PhnD/SsuA/transferrin family substrate-binding protein {ECO:0000313|EMBL:MCC0177545.1};
GN ORFNames=I4641_11205 {ECO:0000313|EMBL:MCC0177545.1};
OS Waterburya agarophytonicola KI4.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
OC Hyellaceae; Waterburya; Waterburya agarophytonicola.
OX NCBI_TaxID=2874699 {ECO:0000313|EMBL:MCC0177545.1, ECO:0000313|Proteomes:UP000729733};
RN [1] {ECO:0000313|EMBL:MCC0177545.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KI4 {ECO:0000313|EMBL:MCC0177545.1};
RX PubMed=34674103;
RA Bonthond G., Shalygin S., Bayer T., Weinberger F.;
RT "Draft genome and description of Waterburya agarophytonicola gen. nov. sp.
RT nov. (Pleurocapsales, Cyanobacteria): a seaweed symbiont.";
RL Antonie Van Leeuwenhoek 0:0-0(2021).
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:MCC0177545.1}.
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DR EMBL; JADWDC010000024; MCC0177545.1; -; Genomic_DNA.
DR RefSeq; WP_229640609.1; NZ_JADWDC010000024.1.
DR AlphaFoldDB; A0A964BTG3; -.
DR Proteomes; UP000729733; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR PANTHER; PTHR32089:SF114; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF12974; Phosphonate-bd; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000729733};
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 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 415..466
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 471..707
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 386..427
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 752 AA; 81679 MW; 99FDC5D786007E16 CRC64;
MLNNLSHQSN SSIKPQKSGF SKNNWKSGIL ILTFGSLILP IANLPLLGSL HPLLTPKVVA
QETPTATPPQ ETKLVKIGIL SKEDTDLTIA QWQPTIDYLS KTIPGYTFEL VPTGFEGMYD
LANSNGANFY IINSGMYVDF EARHGANRIA TLKNLRLGKP YTQFGAVIIT KADRDDIDTV
KDLKNKNFMA VSPIAFGGWQ MAEGVLYDEG IKEPEKFFKQ LDYGETHENV IKAVASGQVD
AGTIRTDALE RAVQRGEAKL EDFKIINQQT TEGFPFVHST PLYPEWPFAA AKGNDTELNE
LVAKALFNMS KDSPAAKASK SEGWTVPLNY RPVHELFIDL NIAPYDEIGR LTFVGFLKKY
IWLNIAVVTI VIGLIANAFY TQRKAIIQEK QNQESLNVLN KSLEENAAEQ KKQREELEKA
VVGLMEALEP AADGDLTVRA QLSEGDVGII ADLFNAIVEN LKDIALQVKD SAGQVGSSLK
ENESSIREIA EQAIVEAEQI QATLSSVEEM STSIKDVASN AEKTAIISND AFMSAKEGNT
VMDRTVDSIQ GLRTTIGDTA KKIKRLGESA QQISQVVALI DEIALKTNLL AINASVEAAR
AGELGQGFTA VAEQVGALAE QSANATKEIA QLITGIQQET QEVVVAMETG TSQVVDSTRL
VEATKVSLST VLIKSQEIDL LMKSISQATI SQAETSQAVT EIMMLNSKSS QERSKSSGQV
AQAIQSTTAI LGELQESVAQ FKVSETEEVG AI
//