SLRP_SALT1
ID SLRP_SALT1 Reviewed; 765 AA.
AC D0ZRB2;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=STM14_928;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP SUBCELLULAR LOCATION, AND SECRETION VIA TYPE III SECRETION SYSTEM.
RX PubMed=10861017; DOI=10.1073/pnas.97.13.7539;
RA Miao E.A., Miller S.I.;
RT "A conserved amino acid sequence directing intracellular type III secretion
RT by Salmonella typhimurium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7539-7544(2000).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=12819095; DOI=10.1128/iai.71.7.4052-4058.2003;
RA Haraga A., Miller S.I.;
RT "A Salmonella enterica serovar typhimurium translocated leucine-rich repeat
RT effector protein inhibits NF-kappa B-dependent gene expression.";
RL Infect. Immun. 71:4052-4058(2003).
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:0000250}.
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 -!- SUBUNIT: Interacts with host TXN. {ECO:0000250}.
CC -!- INTERACTION:
CC D0ZRB2; P10599: TXN; Xeno; NbExp=7; IntAct=EBI-10762386, EBI-594644;
CC -!- SUBCELLULAR LOCATION: Secreted. Host cytoplasm. Note=Secreted via type
CC III secretion systems 1 and 2 (SPI-1 and SPI-2 TTSS), and delivered
CC into the host cytoplasm.
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}.
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DR EMBL; CP001363; ACY87425.1; -; Genomic_DNA.
DR RefSeq; WP_000481997.1; NZ_CP043402.1.
DR PDB; 4PUF; X-ray; 3.30 A; A/B=141-765.
DR PDBsum; 4PUF; -.
DR AlphaFoldDB; D0ZRB2; -.
DR SMR; D0ZRB2; -.
DR IntAct; D0ZRB2; 31.
DR MINT; D0ZRB2; -.
DR EnsemblBacteria; ACY87425; ACY87425; STM14_928.
DR KEGG; seo:STM14_928; -.
DR PATRIC; fig|588858.6.peg.962; -.
DR HOGENOM; CLU_018533_1_0_6; -.
DR OMA; ETEIFFR; -.
DR BioCyc; SENT588858:STM14_RS04625-MON; -.
DR PHI-base; PHI:3743; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:AgBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:1903124; P:negative regulation of thioredoxin peroxidase activity; IMP:AgBase.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:AgBase.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:AgBase.
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; 5.
DR PROSITE; PS51450; LRR; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Leucine-rich repeat; Repeat; Secreted;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Virulence.
FT CHAIN 1..765
FT /note="E3 ubiquitin-protein ligase SlrP"
FT /id="PRO_0000391756"
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..453
FT /note="Interaction with target proteins"
FT /evidence="ECO:0000250"
FT REGION 454..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:0000250"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 429..440
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 448..455
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:4PUF"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 478..489
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 493..503
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 512..527
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 529..544
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 550..568
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 575..599
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 607..617
FT /evidence="ECO:0007829|PDB:4PUF"
FT TURN 618..623
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 641..655
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 659..665
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 668..676
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 678..688
FT /evidence="ECO:0007829|PDB:4PUF"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 697..708
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 731..753
FT /evidence="ECO:0007829|PDB:4PUF"
FT HELIX 755..758
FT /evidence="ECO:0007829|PDB:4PUF"
SQ SEQUENCE 765 AA; 86944 MW; 8BEC9FB8CE5CD25D 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
HLPSEITHLN 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
