ID W0MWV5_PSESX Unreviewed; 259 AA.
AC W0MWV5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Lipoprotein {ECO:0000256|RuleBase:RU364102};
GN ORFNames=N018_15450 {ECO:0000313|EMBL:AHG41513.1};
OS Pseudomonas syringae CC1557.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=1357279 {ECO:0000313|EMBL:AHG41513.1, ECO:0000313|Proteomes:UP000019089};
RN [1] {ECO:0000313|EMBL:AHG41513.1, ECO:0000313|Proteomes:UP000019089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC1557 {ECO:0000313|EMBL:AHG41513.1,
RC ECO:0000313|Proteomes:UP000019089};
RA Baltrus D., Hockett K., Karlsrud E., Dougherty K., Nishimura M.;
RT "Interactions Between Genome Architecture and Virulence Genes in
RT Pseudomonas syringae, strain CC1557 as a model.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|ARBA:ARBA00004459}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004459}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the YscJ lipoprotein family.
CC {ECO:0000256|ARBA:ARBA00009509, ECO:0000256|RuleBase:RU364102}.
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DR EMBL; CP007014; AHG41513.1; -; Genomic_DNA.
DR RefSeq; WP_024644542.1; NZ_CP007014.1.
DR AlphaFoldDB; W0MWV5; -.
DR STRING; 1357279.N018_15450; -.
DR KEGG; psyr:N018_15450; -.
DR eggNOG; COG4669; Bacteria.
DR HOGENOM; CLU_073268_0_0_6; -.
DR Proteomes; UP000019089; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.1530; Hypothetical protein rpa1041; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR006182; FliF_N_dom.
DR InterPro; IPR003282; T3SS_HrcJ/YscJ.
DR InterPro; IPR043427; YscJ/FliF.
DR NCBIfam; TIGR02544; III_secr_YscJ; 1.
DR PANTHER; PTHR30046; FLAGELLAR M-RING PROTEIN; 1.
DR PANTHER; PTHR30046:SF2; YOP PROTEINS TRANSLOCATION LIPOPROTEIN J; 1.
DR Pfam; PF01514; YscJ_FliF; 1.
DR PRINTS; PR01338; TYPE3OMKPROT.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237,
KW ECO:0000256|RuleBase:RU364102};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU364102};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364102};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|RuleBase:RU364102};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364102};
KW Transmembrane {ECO:0000256|RuleBase:RU364102};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364102}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU364102"
FT CHAIN 23..259
FT /note="Lipoprotein"
FT /evidence="ECO:0000256|RuleBase:RU364102"
FT /id="PRO_5011019077"
FT TRANSMEM 223..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364102"
FT DOMAIN 27..189
FT /note="Flagellar M-ring N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01514"
SQ SEQUENCE 259 AA; 28062 MW; 33DA477AAB68031F CRC64;
MSKRCRVLRL LIVATLASLL QACDIDLYTN LGEREANAML AVLLRDGIPA SRKVQDNGQL
KVMVDEKRFA QAMAALDDAG LPGQSFSNMG EVFKGNGLVS SPVQERAQMV YALSEELSHT
VSQIDGILSA RVHVVLPDND LLKRVISPSS ASVLVRYDPR TDINVLIPQI KTLVANGISG
LGYDGVSVTA IKAVIPDKAS AQPQLASFFG LWMLEEDVPA ARWLFGTLLL IALVPAGLLG
RQLWQRRRVE GAYVLSDAP
//
