ID D0VFK3_VIBAL Unreviewed; 247 AA.
AC D0VFK3;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Lipoprotein {ECO:0000256|RuleBase:RU364102};
GN Name=vscJ {ECO:0000313|EMBL:ACY41049.1};
GN Synonyms=sctJ {ECO:0000313|EMBL:NMR76112.1};
GN ORFNames=HKB35_21105 {ECO:0000313|EMBL:NMR76112.1};
OS Vibrio alginolyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663 {ECO:0000313|EMBL:ACY41049.1};
RN [1] {ECO:0000313|EMBL:ACY41049.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZJ51 {ECO:0000313|EMBL:ACY41049.1};
RX PubMed=20576689; DOI=10.1099/mic.0.040626-0;
RA Zhao Z., Chen C., Hu C.Q., Ren C.H., Zhao J.J., Zhang L.P., Jiang X.,
RA Luo P., Wang Q.B.;
RT "The type III secretion system of Vibrio alginolyticus induces rapid
RT apoptosis, cell rounding and osmotic lysis of fish cells.";
RL Microbiology 156:2864-2872(2010).
RN [2] {ECO:0000313|EMBL:NMR76112.1, ECO:0000313|Proteomes:UP000565155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vb1636 {ECO:0000313|EMBL:NMR76112.1,
RC ECO:0000313|Proteomes:UP000565155};
RA Zheng Z., Ye L., Chen S.;
RT "Whole-genome sequencing of Vibrio spp. from China reveals different
RT genetic environments of blaCTX-M-14 among diverse lineages.";
RL Submitted (APR-2020) 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; GU074526; ACY41049.1; -; Genomic_DNA.
DR EMBL; JABCMA010000036; NMR76112.1; -; Genomic_DNA.
DR RefSeq; WP_005377203.1; NZ_VTYJ01000016.1.
DR SMR; D0VFK3; -.
DR STRING; 663.BAU10_07895; -.
DR PATRIC; fig|663.71.peg.1723; -.
DR eggNOG; COG4669; Bacteria.
DR Proteomes; UP000565155; Unassembled WGS sequence.
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..19
FT /evidence="ECO:0000256|RuleBase:RU364102"
FT CHAIN 20..247
FT /note="Lipoprotein"
FT /evidence="ECO:0000256|RuleBase:RU364102"
FT /id="PRO_5014485433"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364102"
FT DOMAIN 21..187
FT /note="Flagellar M-ring N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01514"
SQ SEQUENCE 247 AA; 27362 MW; 0E453342848F441C CRC64;
MMNKMRAVFI MLTLFLVGCQ TELYTNVTQK EGNEMLSILL SEGVVATKEP DKDNTVKLMV
DSSQIAFAVD ALKRKGYPRE QFSTLKEVFP KDDLISSPLA ERARLVYAKS QELSSTLSQI
DGVLVARVHV VLEDQDLRPG ERPTPASASV FIKHAADIAL DSYVPQIKLL VNNSIEGLNY
DRISVVMVPS SEVRVATQNN QFKSILSVQV TKETANNLIA ILVFLVAALI GSNIATFTWC
RRNTKRG
//
