PAL_BRUSU
ID PAL_BRUSU Reviewed; 168 AA.
AC P0A3S8; G0K6V7; Q44662;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Peptidoglycan-associated lipoprotein {ECO:0000255|HAMAP-Rule:MF_02204};
DE Short=PAL {ECO:0000255|HAMAP-Rule:MF_02204};
DE AltName: Full=16.5 kDa minor OMP;
DE Short=16 kDa OMP;
DE AltName: Full=Minor outer membrane protein Omp16;
DE AltName: Full=Outer membrane lipoprotein Omp16;
DE Flags: Precursor;
GN Name=pal {ECO:0000255|HAMAP-Rule:MF_02204}; Synonyms=omp16;
GN OrderedLocusNames=BR1695, BS1330_I1689;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10456959; DOI=10.1128/iai.67.9.4960-4962.1999;
RA Tibor A., Decelle B., Letesson J.-J.;
RT "Outer membrane proteins Omp10, Omp16, and Omp19 of Brucella spp. are
RT lipoproteins.";
RL Infect. Immun. 67:4960-4962(1999).
CC -!- FUNCTION: Part of the Tol-Pal system, which plays a role in outer
CC membrane invagination during cell division and is important for
CC maintaining outer membrane integrity. {ECO:0000255|HAMAP-
CC Rule:MF_02204}.
CC -!- SUBUNIT: The Tol-Pal system is composed of five core proteins: the
CC inner membrane proteins TolA, TolQ and TolR, the periplasmic protein
CC TolB and the outer membrane protein Pal. They form a network linking
CC the inner and outer membranes and the peptidoglycan layer.
CC {ECO:0000255|HAMAP-Rule:MF_02204}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_02204}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_02204}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the Pal lipoprotein family. {ECO:0000255|HAMAP-
CC Rule:MF_02204}.
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DR EMBL; AE014291; AAN30595.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM19012.1; -; Genomic_DNA.
DR RefSeq; WP_002966947.1; NZ_KN046804.1.
DR AlphaFoldDB; P0A3S8; -.
DR SMR; P0A3S8; -.
DR EnsemblBacteria; AEM19012; AEM19012; BS1330_I1689.
DR GeneID; 45124999; -.
DR GeneID; 55591316; -.
DR KEGG; bms:BR1695; -.
DR KEGG; bsi:BS1330_I1689; -.
DR PATRIC; fig|204722.21.peg.2404; -.
DR HOGENOM; CLU_016890_9_2_5; -.
DR OMA; TPENAGM; -.
DR PhylomeDB; P0A3S8; -.
DR Proteomes; UP000007104; Chromosome I.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR HAMAP; MF_02204; Pal; 1.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR039001; Pal.
DR InterPro; IPR014169; Pal_lipo_C.
DR Pfam; PF00691; OmpA; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; SSF103088; 1.
DR TIGRFAMs; TIGR02802; Pal_lipo; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell outer membrane; Lipoprotein; Membrane;
KW Palmitate; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204, ECO:0000305"
FT CHAIN 25..168
FT /note="Peptidoglycan-associated lipoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT /id="PRO_0000020130"
FT DOMAIN 51..167
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
SQ SEQUENCE 168 AA; 18233 MW; 17F75F4F05EB1DD8 CRC64;
MRRIQSIARS PIAIALFMSL AVAGCASKKN LPNNAGDLGL GAGAATPGSS QDFTVNVGDR
IFFDLDSSLI RADAQQTLSK QAQWLQRYPQ YSITIEGHAD ERGTREYNLA LGQRRAAATR
DFLASRGVPT NRMRTISYGN ERPVAVCDAD TCWSQNRRAV TVLNGAGR
