Y1468_THEMA
ID Y1468_THEMA Reviewed; 288 AA.
AC Q9X1H9;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Fatty acid-binding protein TM_1468;
GN OrderedLocusNames=TM_1468;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2] {ECO:0007744|PDB:1MGP}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PALMITATE, FUNCTION,
RP AND SUBUNIT.
RX PubMed=12577257; DOI=10.1002/prot.10305;
RA Schulze-Gahmen U., Pelaschier J., Yokota H., Kim R., Kim S.-H.;
RT "Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima,
RT reveals its function as a fatty acid-binding protein.";
RL Proteins 50:526-530(2003).
RN [3] {ECO:0007744|PDB:1VPV}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH PALMITATE.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of UPF0230 protein TM1468 (TM1468) from Thermotoga
RT maritima at 2.45 A resolution.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Binds long-chain fatty acids, such as palmitate, and may play
CC a role in lipid transport or fatty acid metabolism.
CC {ECO:0000269|PubMed:12577257}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:12577257, ECO:0000305|Ref.3}.
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DR EMBL; AE000512; AAD36536.1; -; Genomic_DNA.
DR PIR; E72246; E72246.
DR RefSeq; NP_229268.1; NC_000853.1.
DR RefSeq; WP_004081771.1; NZ_CP011107.1.
DR PDB; 1MGP; X-ray; 2.00 A; A=1-288.
DR PDB; 1VPV; X-ray; 2.45 A; A/B=1-288.
DR PDBsum; 1MGP; -.
DR PDBsum; 1VPV; -.
DR AlphaFoldDB; Q9X1H9; -.
DR SMR; Q9X1H9; -.
DR STRING; 243274.THEMA_06960; -.
DR DrugBank; DB03796; Palmitic Acid.
DR DNASU; 897743; -.
DR EnsemblBacteria; AAD36536; AAD36536; TM_1468.
DR KEGG; tma:TM1468; -.
DR eggNOG; COG1307; Bacteria.
DR InParanoid; Q9X1H9; -.
DR OMA; MALGFCA; -.
DR OrthoDB; 1288126at2; -.
DR EvolutionaryTrace; Q9X1H9; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1180.10; -; 1.
DR InterPro; IPR003797; DegV.
DR InterPro; IPR043168; DegV_C.
DR Pfam; PF02645; DegV; 1.
DR TIGRFAMs; TIGR00762; DegV; 1.
DR PROSITE; PS51482; DEGV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid-binding; Reference proteome.
FT CHAIN 1..288
FT /note="Fatty acid-binding protein TM_1468"
FT /id="PRO_0000209816"
FT DOMAIN 3..283
FT /note="DegV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT BINDING 63
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:12577257,
FT ECO:0007744|PDB:1MGP, ECO:0007744|PDB:1VPV"
FT BINDING 96
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:12577257,
FT ECO:0007744|PDB:1MGP, ECO:0007744|PDB:1VPV"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1MGP"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:1MGP"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 254..263
FT /evidence="ECO:0007829|PDB:1MGP"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:1MGP"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:1MGP"
SQ SEQUENCE 288 AA; 32575 MW; 1CF1D341AF278E2E CRC64;
MKVKILVDST ADVPFSWMEK YDIDSIPLYV VWEDGRSEPD EREPEEIMNF YKRIREAGSV
PKTSQPSVED FKKRYLKYKE EDYDVVLVLT LSSKLSGTYN SAVLASKEVD IPVYVVDTLL
ASGAIPLPAR VAREMLENGA TIEEVLKKLD ERMKNKDFKA IFYVSNFDYL VKGGRVSKFQ
GFVGNLLKIR VCLHIENGEL IPYRKVRGDK KAIEALIEKL REDTPEGSKL RVIGVHADNE
AGVVELLNTL RKSYEVVDEI ISPMGKVITT HVGPGTVGFG IEVLERKR
