SCTN_SINFN
ID SCTN_SINFN Reviewed; 451 AA.
AC P55717;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Type 3 secretion system ATPase {ECO:0000250|UniProtKB:P0A1C1};
DE Short=T3SS ATPase {ECO:0000250|UniProtKB:P0A1C1};
DE EC=7.4.2.8 {ECO:0000250|UniProtKB:P0A1C1};
GN Name=sctN {ECO:0000250|UniProtKB:P0A1C1}; OrderedLocusNames=NGR_a00640;
GN ORFNames=y4yI;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- FUNCTION: ATPase component of the type III secretion system (T3SS),
CC also called injectisome, which is used to inject bacterial effector
CC proteins into eukaryotic host cells (By similarity). Acts as a
CC molecular motor to provide the energy that is required for the export
CC of proteins (By similarity). Required for type III secretion apparatus
CC (T3SA) formation, proper protein secretion, host cell invasion and
CC virulence (By similarity). May play a critical role in T3SS substrate
CC recognition, disassembly of the effector/chaperone complex and
CC unfolding of the effector in an ATP-dependent manner prior to secretion
CC (By similarity). {ECO:0000250|UniProtKB:P0A1B9,
CC ECO:0000250|UniProtKB:P0A1C1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000250|UniProtKB:P0A1C1};
CC -!- SUBUNIT: The core secretion machinery of the T3SS is composed of
CC approximately 20 different proteins, including cytoplasmic components,
CC a base, an export apparatus and a needle (By similarity). This subunit
CC is part of the cytosolic complex (By similarity). Forms homohexamers
CC (By similarity). {ECO:0000250|UniProtKB:P0A1C1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A1C1}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000305}.
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DR EMBL; U00090; AAB91948.1; -; Genomic_DNA.
DR RefSeq; NP_444161.1; NC_000914.2.
DR RefSeq; WP_010875105.1; NC_000914.2.
DR AlphaFoldDB; P55717; -.
DR SMR; P55717; -.
DR STRING; 394.NGR_a00640; -.
DR PRIDE; P55717; -.
DR EnsemblBacteria; AAB91948; AAB91948; NGR_a00640.
DR KEGG; rhi:NGR_a00640; -.
DR PATRIC; fig|394.7.peg.60; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_5; -.
DR OMA; RLCHHIA; -.
DR OrthoDB; 875807at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030257; C:type III protein secretion system complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005714; ATPase_T3SS_FliI/YscN.
DR InterPro; IPR013380; ATPase_T3SS_SCTN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040627; T3SS_ATPase_C.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF18269; T3SS_ATPase_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01026; fliI_yscN; 1.
DR TIGRFAMs; TIGR02546; III_secr_ATP; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Plasmid; Protein transport;
KW Reference proteome; Translocase; Transport; Virulence.
FT CHAIN 1..451
FT /note="Type 3 secretion system ATPase"
FT /id="PRO_0000144711"
FT BINDING 184..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1C1"
SQ SEQUENCE 451 AA; 48766 MW; 259176AAD426DA30 CRC64;
MITPVPQHNS LEGTPLEPAI SSLWSTAKRI DTRVVRGRIT RAVGTLIHAV LPEARIGELC
LLQDTRTGLS LEAEVIGLLD NGVLLTPIGG LAGLSSRAEV VSTGRMREVP IGPDLLGRVI
DSRCRPLDGK GEVKTTEVRP LHGRAPNPMT RRMVERPFPL GVRALDGLLT CGEGQRIGIY
GEPGGGKSTL ISQIVKGAAA DVVIVALIGE RGREVREFVE RHLGEEGLRR AIVVVETSDR
SATERAQCAP MATALAEYFR EQGLRVALLL DSLTRFCRAM REIGLAAGEP PTRRGFPPSV
FAALPGLLER AGLGERGSIT AFYTVLVEGD GTGDPIAEES RGILDGHIVL SRALAARSHF
PAIDVLQSRS RVMDAVVSET HRKAASFFRD LLARYAECEF LINVGEYKQG GDPLTDRAVA
SIGELKEFLR QSEDEVSDFE ETVGWMSRLT S
