HXCR_PSEAE
ID HXCR_PSEAE Reviewed; 469 AA.
AC Q9I5N9;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Type II secretion system protein HxcR {ECO:0000303|PubMed:18282104};
DE EC=7.4.2.8 {ECO:0000250|UniProtKB:P37093};
GN Name=hxcR {ECO:0000303|PubMed:11985723}; OrderedLocusNames=PA0686;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=11985723; DOI=10.1046/j.1365-2958.2002.02759.x;
RA Ball G., Durand E., Lazdunski A., Filloux A.;
RT "A novel type II secretion system in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 43:475-485(2002).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=18282104; DOI=10.1371/journal.ppat.0040043;
RA Zaborina O., Holbrook C., Chen Y., Long J., Zaborin A., Morozova I.,
RA Fernandez H., Wang Y., Turner J.R., Alverdy J.C.;
RT "Structure-function aspects of PstS in multi-drug-resistant Pseudomonas
RT aeruginosa.";
RL PLoS Pathog. 4:E43-E43(2008).
CC -!- FUNCTION: ATPase component of the type II secretion system required for
CC the energy-dependent secretion of extracellular factors from the
CC periplasm (By similarity). Acts as a molecular motor to provide the
CC energy that is required for the export of proteins (By similarity). The
CC Hxc system is involved in the secretion of low-molecular-weight
CC alkaline phosphatase L-AP (LapA) (PubMed:11985723). Is probably also
CC involved in the secretion of the phosphate-binding protein PstS
CC (PubMed:18282104). {ECO:0000250|UniProtKB:P37093,
CC ECO:0000269|PubMed:11985723, ECO:0000269|PubMed:18282104}.
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:P37093};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by phosphate limitation.
CC {ECO:0000269|PubMed:11985723, ECO:0000269|PubMed:18282104}.
CC -!- DISRUPTION PHENOTYPE: Mutant cannot secrete the low-molecular-weight
CC alkaline phosphatase LapA (PubMed:11985723). Deletion mutant shows
CC decreased ability to express outer surface PstS, but not intracellular
CC PstS (PubMed:18282104). {ECO:0000269|PubMed:11985723,
CC ECO:0000269|PubMed:18282104}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04075.1; -; Genomic_DNA.
DR PIR; D83561; D83561.
DR RefSeq; NP_249377.1; NC_002516.2.
DR RefSeq; WP_003112722.1; NZ_QZGE01000025.1.
DR AlphaFoldDB; Q9I5N9; -.
DR SMR; Q9I5N9; -.
DR STRING; 287.DR97_1433; -.
DR PaxDb; Q9I5N9; -.
DR EnsemblBacteria; AAG04075; AAG04075; PA0686.
DR GeneID; 880808; -.
DR KEGG; pae:PA0686; -.
DR PATRIC; fig|208964.12.peg.718; -.
DR PseudoCAP; PA0686; -.
DR HOGENOM; CLU_013446_2_0_6; -.
DR InParanoid; Q9I5N9; -.
DR OMA; LIRKPHG; -.
DR PhylomeDB; Q9I5N9; -.
DR BioCyc; PAER208964:G1FZ6-696-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015627; C:type II protein secretion system complex; IMP:PseudoCAP.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
DR Gene3D; 3.30.300.160; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR013369; T2SS_GspE.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF160246; SSF160246; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02533; type_II_gspE; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Protein transport;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..469
FT /note="Type II secretion system protein HxcR"
FT /id="PRO_0000431614"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 469 AA; 50978 MW; DD2A54CEE3FF1DF0 CRC64;
MSLLPYAWAK AQRALLRPGE HGATLLVSPR TPGWAISEVR QRHAPASLES VRDDELDTLL
ASAYSDTGSA AAVVGAAESE VDLDRLMDDI PEVTDLLDTQ DGAPVIRMIN ALLTQAARDE
ASDIHIEPFE THSVVRYRVD GALRDVVAPR KALHAALVSR IKIMAQLDIA EKRLPQDGRI
ALRVAGRPID IRVSTVPTGH GERVVMRLLD KQAGRLRLET LGMAPGVLAP LDNLIRQPHG
IVLVTGPTGS GKTTTLYAAL ARLDASTSNI LTVEDPVEYD LPGISQIQVN ARIDMTFAVA
LRAILRQDPD IIMIGEIRDL ETAQIAVQAS LTGHLVLATL HTNDAVSAVT RLVDMGVEPF
LLASSMLGVL AQRLVRRLCT HCRVEEDGGW RAVGCPACNQ TGYSGRTGIH ELFVIDDEIR
RLVHQGRAEQ DLREAARAAG MRSMREDGER WIASGSTTLE EILRVTRDA
