ID B1FJW2_9BURK Unreviewed; 244 AA.
AC B1FJW2;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Lipoprotein {ECO:0000256|RuleBase:RU364102};
GN ORFNames=BamIOP4010DRAFT_4323 {ECO:0000313|EMBL:EDT02178.1};
OS Burkholderia ambifaria IOP40-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396596 {ECO:0000313|EMBL:EDT02178.1, ECO:0000313|Proteomes:UP000005463};
RN [1] {ECO:0000313|EMBL:EDT02178.1, ECO:0000313|Proteomes:UP000005463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOP40-10 {ECO:0000313|EMBL:EDT02178.1,
RC ECO:0000313|Proteomes:UP000005463};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria
RT IOP40-10.";
RL Submitted (MAR-2008) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDT02178.1}.
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DR EMBL; ABLC01000131; EDT02178.1; -; Genomic_DNA.
DR AlphaFoldDB; B1FJW2; -.
DR PATRIC; fig|396596.7.peg.3211; -.
DR Proteomes; UP000005463; 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.
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 TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364102"
FT DOMAIN 11..176
FT /note="Flagellar M-ring N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01514"
SQ SEQUENCE 244 AA; 25877 MW; A37700B1686AAFC0 CRC64;
MLVLSLAACK QELYGQLSES DCNEMVAALL SSGVDAQKST PDGGKTWSVS VDEKQIVHAV
EVLRARGIPR KKFDDLGSLF KKDGLVSTPT EERVRFIYGL SQELDDTLSK IDGVVVARVQ
IVLPNNDPLA QSVKPSSASV FIKYRPDANL ERMTPAIKNL VVHSIEGLTY DQVSVTSVPA
DAPDAPARPR RQGGWIVYAG GALGVLLLMI AGGFALLRGT LLKGGGGLAG LLARRTGRAA
KAPA
//
