SLRP_SALTY
ID SLRP_SALTY Reviewed; 765 AA.
AC Q8ZQQ2; Q9XCV2;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=E3 ubiquitin-protein ligase SlrP;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SlrP {ECO:0000305};
DE AltName: Full=Secreted effector protein SlrP;
GN Name=slrP; OrderedLocusNames=STM0800;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=10569754; DOI=10.1128/iai.67.12.6385-6393.1999;
RA Tsolis R.M., Townsend S.M., Miao E.A., Miller S.I., Ficht T.A., Adams L.G.,
RA Baumler A.J.;
RT "Identification of a putative Salmonella enterica serotype typhimurium host
RT range factor with homology to IpaH and YopM by signature-tagged
RT mutagenesis.";
RL Infect. Immun. 67:6385-6393(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION AS AN UBIQUITIN LIGASE, ACTIVITY REGULATION, INTERACTION WITH HOST
RP TXN, AND MUTAGENESIS OF CYS-546.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=19690162; DOI=10.1074/jbc.m109.010363;
RA Bernal-Bayard J., Ramos-Morales F.;
RT "Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase for
RT mammalian thioredoxin.";
RL J. Biol. Chem. 284:27587-27595(2009).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. This protein is an E3
CC ubiquitin ligase that interferes with host's ubiquitination pathway.
CC Can ubiquitinate both ubiquitin and host TXN (thioredoxin). Leads to
CC significant decrease of thioredoxin activity and increase of host cell
CC death. {ECO:0000269|PubMed:19690162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- ACTIVITY REGULATION: Binding to TXN is inhibited by hydrogen peroxide
CC in vitro. {ECO:0000269|PubMed:19690162}.
CC -!- SUBUNIT: Interacts with host TXN. {ECO:0000269|PubMed:19690162}.
CC -!- INTERACTION:
CC Q8ZQQ2; Q9UBS4: DNAJB11; Xeno; NbExp=4; IntAct=EBI-10712653, EBI-713113;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Note=Secreted via type III secretion systems 1 and 2
CC (SPI-1 and SPI-2 TTSS), and delivered into the host cytoplasm.
CC {ECO:0000250}.
CC -!- DOMAIN: The LRR (leucine-rich repeat) domain forms a slightly curved
CC solenoid and may mediate interaction with target proteins.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating
CC enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LRR-containing bacterial E3 ligase family.
CC {ECO:0000305}.
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; AF127079; AAD39928.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19737.1; -; Genomic_DNA.
DR RefSeq; NP_459778.1; NC_003197.2.
DR RefSeq; WP_000482001.1; NC_003197.2.
DR AlphaFoldDB; Q8ZQQ2; -.
DR SMR; Q8ZQQ2; -.
DR IntAct; Q8ZQQ2; 1.
DR STRING; 99287.STM0800; -.
DR PaxDb; Q8ZQQ2; -.
DR EnsemblBacteria; AAL19737; AAL19737; STM0800.
DR GeneID; 1252320; -.
DR KEGG; stm:STM0800; -.
DR PATRIC; fig|99287.12.peg.834; -.
DR HOGENOM; CLU_018533_1_0_6; -.
DR OMA; ETEIFFR; -.
DR PhylomeDB; Q8ZQQ2; -.
DR BioCyc; SENT99287:STM0800-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:AgBase.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IPI:AgBase.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:AgBase.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR032674; LRR_E3_ligase_N.
DR InterPro; IPR029487; NEL_dom.
DR Pfam; PF14496; NEL; 1.
DR Pfam; PF12468; TTSSLRR; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR PROSITE; PS51450; LRR; 9.
PE 1: Evidence at protein level;
KW Host cytoplasm; Leucine-rich repeat; Reference proteome; Repeat; Secreted;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Virulence.
FT CHAIN 1..765
FT /note="E3 ubiquitin-protein ligase SlrP"
FT /id="PRO_0000391755"
FT REPEAT 200..219
FT /note="LRR 1"
FT REPEAT 221..242
FT /note="LRR 2"
FT REPEAT 243..262
FT /note="LRR 3"
FT REPEAT 263..284
FT /note="LRR 4"
FT REPEAT 285..305
FT /note="LRR 5"
FT REPEAT 306..325
FT /note="LRR 6"
FT REPEAT 326..346
FT /note="LRR 7"
FT REPEAT 347..368
FT /note="LRR 8"
FT REPEAT 369..389
FT /note="LRR 9"
FT REPEAT 390..410
FT /note="LRR 10"
FT REGION 1..451
FT /note="Interaction with target proteins"
FT /evidence="ECO:0000250"
FT REGION 452..461
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 462..765
FT /note="E3 ubiquitin-protein ligase catalytic domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 546
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 546
FT /note="C->A: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:19690162"
FT CONFLICT 168
FT /note="A -> P (in Ref. 1; AAD39928)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="G -> E (in Ref. 1; AAD39928)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="F -> V (in Ref. 1; AAD39928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 86872 MW; 529A0B64ED55CCF6 CRC64;
MFNITNIQST ARHQSISNEA STEVPLKEEI WNKISAFFSS EHQVEAQNCI AYLCHPPETA
SPEEIKSKFE CLRMLAFPAY ADNIQYSRGG ADQYCILSEN SQEILSIVFN TEGYTVEGGG
KSVTYTRVTE SEQASSASGS KDAVNYELIW SEWVKEAPAK EAANREEAVQ RMRDCLKNNK
TELRLKILGL TTIPAYIPEQ ITTLILDNNE LKSLPENLQG NIKTLYANSN QLTSIPATLP
DTIQEMELSI NRITELPERL PSALQSLDLF HNKISCLPEN LPEELRYLSV YDNSIRTLPA
HLPSGITHLN VQSNSLTALP ETLPPGLKTL EAGENALTSL PASLPPELQV LDVSKNQITV
LPETLPPTIT TLDVSRNALT NLPENLPAAL QIMQASRNNL VRLPESLPHF RGEGPQPTRI
IVEYNPFSER TIQNMQRLMS SVDYQGPRVL FAMGDFSIVR VTRPLHQAVQ GWLTSLEEED
VNQWRAFEAE ANAAAFSGFL DYLGDTQNTR HPDFKEQVSA WLMRLAEDSA LRETVFIIAM
NATISCEDRV TLAYHQMQEA TLVHDAERGA FDSHLAELIM AGREIFRLEQ IESLAREKVK
RLFFIDEVEV FLGFQNQLRE SLSLTTMTRD MRFYNVSGIT ESDLDEAEIR IKMAENRDFH
KWFALWGPWH KVLERIAPEE WREMMAKRDE CIETDEYQSR VNAELEDLRI ADDSDAERTT
EVQMDAERAI GIKIMEEINQ TLFTEIMENI LLKKEVSSLM SAYWR
