DEGV_BACSU
ID DEGV_BACSU Reviewed; 281 AA.
AC P32436;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein DegV;
GN Name=degV; Synonyms=yviA; OrderedLocusNames=BSU35480;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8412657; DOI=10.1111/j.1365-2958.1993.tb01674.x;
RA Londono-Vallejo J.A., Dubnau D.;
RT "comF, a Bacillus subtilis late competence locus, encodes a protein similar
RT to ATP-dependent RNA/DNA helicases.";
RL Mol. Microbiol. 9:119-131(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969505; DOI=10.1099/13500872-142-11-3079;
RA Soldo B., Lazarevic V., Mauel C., Karamata D.;
RT "Sequence of the 305 degrees-307 degrees region of the Bacillus subtilis
RT chromosome.";
RL Microbiology 142:3079-3088(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
RX PubMed=3141378; DOI=10.1128/jb.170.11.5102-5109.1988;
RA Henner D.J., Yang M., Ferrari E.;
RT "Localization of Bacillus subtilis sacU(Hy) mutations to two linked genes
RT with similarities to the conserved procaryotic family of two-component
RT signalling systems.";
RL J. Bacteriol. 170:5102-5109(1988).
RN [5] {ECO:0007744|PDB:3FYS}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH PALMITIC ACID,
RP FUNCTION, AND SUBUNIT.
RX PubMed=19390149; DOI=10.1107/s0907444909007756;
RA Nan J., Zhou Y., Yang C., Brostromer E., Kristensen O., Su X.D.;
RT "Structure of a fatty-acid-binding protein from Bacillus subtilis
RT determined by sulfur-SAD phasing using in-house chromium radiation.";
RL Acta Crystallogr. D 65:440-448(2009).
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:19390149}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:19390149}.
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DR EMBL; Z18629; CAA79225.1; -; Genomic_DNA.
DR EMBL; U56901; AAC44939.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15565.1; -; Genomic_DNA.
DR EMBL; M23558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; I40386; D30191.
DR RefSeq; NP_391428.1; NC_000964.3.
DR RefSeq; WP_003244125.1; NZ_JNCM01000033.1.
DR PDB; 3FYS; X-ray; 2.50 A; A=1-281.
DR PDBsum; 3FYS; -.
DR AlphaFoldDB; P32436; -.
DR SMR; P32436; -.
DR STRING; 224308.BSU35480; -.
DR PaxDb; P32436; -.
DR PRIDE; P32436; -.
DR EnsemblBacteria; CAB15565; CAB15565; BSU_35480.
DR GeneID; 936763; -.
DR KEGG; bsu:BSU35480; -.
DR PATRIC; fig|224308.179.peg.3839; -.
DR eggNOG; COG1307; Bacteria.
DR InParanoid; P32436; -.
DR OMA; MALGFCA; -.
DR PhylomeDB; P32436; -.
DR BioCyc; BSUB:BSU35480-MON; -.
DR EvolutionaryTrace; P32436; -.
DR Proteomes; UP000001570; 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..281
FT /note="Protein DegV"
FT /id="PRO_0000209751"
FT DOMAIN 3..280
FT /note="DegV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT BINDING 61
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:19390149,
FT ECO:0007744|PDB:3FYS"
FT BINDING 93
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:19390149,
FT ECO:0007744|PDB:3FYS"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3FYS"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:3FYS"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:3FYS"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:3FYS"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:3FYS"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:3FYS"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 206..221
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:3FYS"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:3FYS"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:3FYS"
SQ SEQUENCE 281 AA; 31580 MW; 737B6DC65D6FCE64 CRC64;
MNIAVVTDST AYIPKEMREQ HQIHMIPLQV VFREETYREE IELDWKSFYE EVKKHNELPT
TSQPPIGELV ALYEELGKSY DAVISIHLSS GISGTFSSAA AADSMVDNID VYPFDSEISC
LAQGFYALKA AELIKNGASS PEDIIKELEE MKKTVRAYFM VDDLAHLQRG GRLSSAQAFI
GSLLKVKPIL HFDNKVIVPF EKIRTRKKAI SRIYELLDED ASKGLPMRAA VIHANREEEA
AKIIEELSAK YPHVEFYNSY FGAVIGTHLG EGALGICWCF K
