PAL_BRUAB
ID PAL_BRUAB Reviewed; 168 AA.
AC P0A3S9; Q44662; Q57BI5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-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=BruAb1_1680;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 53-58.
RC STRAIN=544 / Biovar 1;
RX PubMed=8063379; DOI=10.1128/iai.62.9.3633-3639.1994;
RA Tibor A., Weynants V., Denoel P., Lichtfouse B., De Bolle X., Saman E.,
RA Limet J.N., Letesson J.-J.;
RT "Molecular cloning, nucleotide sequence, and occurrence of a 16.5-
RT kilodalton outer membrane protein of Brucella abortus with similarity to
RT pal lipoproteins.";
RL Infect. Immun. 62:3633-3639(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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; L27996; AAA59360.1; -; Genomic_DNA.
DR EMBL; AE017223; AAX74999.1; -; Genomic_DNA.
DR PIR; I40346; I40346.
DR RefSeq; WP_002966947.1; NC_006932.1.
DR AlphaFoldDB; P0A3S9; -.
DR SMR; P0A3S9; -.
DR EnsemblBacteria; AAX74999; AAX74999; BruAb1_1680.
DR GeneID; 45124999; -.
DR GeneID; 55591316; -.
DR KEGG; bmb:BruAb1_1680; -.
DR HOGENOM; CLU_016890_9_2_5; -.
DR OMA; TPENAGM; -.
DR Proteomes; UP000000540; 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; Direct protein sequencing;
KW Lipoprotein; Membrane; 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_0000020128"
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
