ID   CSHA_STAS1              Reviewed;         506 AA.
AC   Q49Z29;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase CshA {ECO:0000255|HAMAP-Rule:MF_01493};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_01493};
GN   Name=cshA {ECO:0000255|HAMAP-Rule:MF_01493}; OrderedLocusNames=SSP0802;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC   -!- FUNCTION: DEAD-box RNA helicase possibly involved in RNA degradation.
CC       Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase
CC       activity. {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01493};
CC   -!- SUBUNIT: Oligomerizes, may be a member of the RNA degradosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
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DR   EMBL; AP008934; BAE17947.1; -; Genomic_DNA.
DR   RefSeq; WP_011302697.1; NZ_MTGA01000032.1.
DR   AlphaFoldDB; Q49Z29; -.
DR   SMR; Q49Z29; -.
DR   STRING; 342451.SSP0802; -.
DR   EnsemblBacteria; BAE17947; BAE17947; SSP0802.
DR   GeneID; 66866958; -.
DR   KEGG; ssp:SSP0802; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_21_1_9; -.
DR   OMA; EHKDGQR; -.
DR   OrthoDB; 626183at2; -.
DR   Proteomes; UP000006371; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01493; DEAD_helicase_CshA; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR030880; DEAD_helicase_CshA.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Stress response.
FT   CHAIN           1..506
FT                   /note="DEAD-box ATP-dependent RNA helicase CshA"
FT                   /id="PRO_0000284830"
FT   DOMAIN          33..203
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   DOMAIN          214..375
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   REGION          434..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2..30
FT                   /note="Q motif"
FT   MOTIF           150..153
FT                   /note="DEAD box"
FT   COMPBIAS        458..506
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
SQ   SEQUENCE   506 AA;  56734 MW;  41B8FE76F360D803 CRC64;
     MQNFKELGIS DKMAETLQSM GFNEATPIQK ESIPLALEGK DVLGQAQTGT GKTGAFGIPL
     IEKVADQEGV QSLILAPTRE LAMQVAESLK AFAKGQNIQV VTVFGGMPID RQIKALKKGP
     QIVVGTPGRV IDHLNRRTLK TNDIHTLILD EADEMMNMGF IDDMKFIMDK IPAEQRQTML
     FSATMPKAIQ TLVQQFMKSP VIVKTMNNEM SDPQIEEYYT IVKELEKFDT FTSFLDVHQP
     ELAIVFGRTK RRVDELTSAL ISKGYKAEGL HGDITQAKRL EVLKKFKNDQ LDILVATDVA
     ARGLDISGVS HVYNFDIPQD TESYTHRIGR TGRAGKKGVA ITFVNPIEMD YIRQIEQANK
     RQMTALRPPH RKEVLKAREN DIKGKVQNWM SRDNEPRLQR IATELLGEYN DVDLIASLLQ
     ELVESNDEVD VQLTFEKPLS RGKGRQGKGG PKRGGNHKRG GGKFDNKNRR SGKGGFNNKK
     KNDRPSSDRN NNKKSMKGRT FADHKK