CSAA_BACSU
ID CSAA_BACSU Reviewed; 110 AA.
AC P37584;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable chaperone CsaA {ECO:0000303|PubMed:10816431};
GN Name=csaA; OrderedLocusNames=BSU19040;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POSSIBLE FUNCTION.
RC STRAIN=168 / DB104;
RX PubMed=1435734; DOI=10.1007/bf00286185;
RA Mueller J., Walter F., van Dijl J.M., Behnke D.;
RT "Suppression of the growth and export defects of an Escherichia coli
RT secA(Ts) mutant by a gene cloned from Bacillus subtilis.";
RL Mol. Gen. Genet. 235:89-96(1992).
RN [2]
RP SEQUENCE REVISION.
RA Mueller J.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT terC and odhAB loci cloned in a yeast artificial chromosome.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / DB104;
RX PubMed=10816431; DOI=10.1042/bj3480367;
RA Mueller J.P., Ozegowski J., Vettermann S., Swaving J., Van Wely K.H.,
RA Driessen A.J.;
RT "Interaction of Bacillus subtilis CsaA with SecA and precursor proteins.";
RL Biochem. J. 348:367-373(2000).
RN [6]
RP SUBUNIT.
RX PubMed=13129613; DOI=10.1016/s0378-1097(03)00578-0;
RA Linde D., Volkmer-Engert R., Schreiber S., Mueller J.P.;
RT "Interaction of the Bacillus subtilis chaperone CsaA with the secretory
RT protein YvaY.";
RL FEMS Microbiol. Lett. 226:93-100(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RX PubMed=17372352; DOI=10.1107/s0907444907005045;
RA Shapova Y.A., Paetzel M.;
RT "Crystallographic analysis of Bacillus subtilis CsaA.";
RL Acta Crystallogr. D 63:478-485(2007).
CC -!- FUNCTION: Can suppress growth and secretion defects in E.coli secA and
CC secB mutants (PubMed:1435734). Probably a molecular chaperone for
CC exported proteins or may act by stabilizing the SecA protein
CC (PubMed:1435734, PubMed:10816431). {ECO:0000305|PubMed:10816431,
CC ECO:0000305|PubMed:1435734}.
CC -!- SUBUNIT: Homodimer (PubMed:17372352). Probably binds SecA and prePhoB
CC (PubMed:10816431). Probably interacts with proSdpC (PubMed:13129613).
CC {ECO:0000269|PubMed:10816431, ECO:0000269|PubMed:13129613,
CC ECO:0000269|PubMed:17372352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10816431}.
CC -!- INDUCTION: Present in exponentially growing cells (at protein level).
CC {ECO:0000269|PubMed:10816431}.
CC -!- DISRUPTION PHENOTYPE: Grows normally, reduced secretion of SdpC
CC (formerly YvaY) and another 36 kDa protein.
CC {ECO:0000269|PubMed:10816431}.
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; X58387; CAA41277.1; -; Genomic_DNA.
DR EMBL; AF027868; AAB84466.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13796.1; -; Genomic_DNA.
DR PIR; E69607; E69607.
DR RefSeq; NP_389785.1; NC_000964.3.
DR RefSeq; WP_004399582.1; NZ_JNCM01000036.1.
DR PDB; 2NZH; X-ray; 1.90 A; A/B=1-110.
DR PDB; 2NZO; X-ray; 2.00 A; A/B/C/D=1-110.
DR PDBsum; 2NZH; -.
DR PDBsum; 2NZO; -.
DR AlphaFoldDB; P37584; -.
DR SMR; P37584; -.
DR STRING; 224308.BSU19040; -.
DR PaxDb; P37584; -.
DR PRIDE; P37584; -.
DR EnsemblBacteria; CAB13796; CAB13796; BSU_19040.
DR GeneID; 939631; -.
DR KEGG; bsu:BSU19040; -.
DR PATRIC; fig|224308.179.peg.2082; -.
DR eggNOG; COG0073; Bacteria.
DR InParanoid; P37584; -.
DR OMA; FPEARNP; -.
DR PhylomeDB; P37584; -.
DR BioCyc; BSUB:BSU19040-MON; -.
DR EvolutionaryTrace; P37584; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR008231; CsaA.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR PANTHER; PTHR11586:SF37; PTHR11586:SF37; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR02222; chap_CsaA; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Protein transport; Reference proteome;
KW RNA-binding; Translocation; Transport; tRNA-binding.
FT CHAIN 1..110
FT /note="Probable chaperone CsaA"
FT /id="PRO_0000079389"
FT DOMAIN 6..110
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 12..23
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:2NZH"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2NZH"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2NZH"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:2NZH"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2NZH"
SQ SEQUENCE 110 AA; 11907 MW; DC263A1D3B194A43 CRC64;
MAVIDDFEKL DIRTGTIVKA EEFPEARVPA IKLVIDFGTE IGIKQSSAQI TKRYKPEGLI
NKQVIAVVNF PPRRIAGFKS EVLVLGGIPG QGDVVLLQPD QPVPNGTKIG
