ID I0HN66_RUBGI Unreviewed; 181 AA.
AC I0HN66;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Peptidoglycan-associated lipoprotein {ECO:0000256|HAMAP-Rule:MF_02204};
DE Short=PAL {ECO:0000256|HAMAP-Rule:MF_02204};
GN Name=pal {ECO:0000256|HAMAP-Rule:MF_02204,
GN ECO:0000313|EMBL:BAL94453.1};
GN OrderedLocusNames=RGE_11120 {ECO:0000313|EMBL:BAL94453.1};
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL94453.1, ECO:0000313|Proteomes:UP000007883};
RN [1] {ECO:0000313|EMBL:BAL94453.1, ECO:0000313|Proteomes:UP000007883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX PubMed=22689232; DOI=10.1128/JB.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.P.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(2012).
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:0000256|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:0000256|HAMAP-Rule:MF_02204}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_02204}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_02204}.
CC -!- SIMILARITY: Belongs to the Pal lipoprotein family. {ECO:0000256|HAMAP-
CC Rule:MF_02204}.
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DR EMBL; AP012320; BAL94453.1; -; Genomic_DNA.
DR RefSeq; WP_014427324.1; NC_017075.1.
DR AlphaFoldDB; I0HN66; -.
DR STRING; 983917.RGE_11120; -.
DR KEGG; rge:RGE_11120; -.
DR PATRIC; fig|983917.3.peg.1089; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016890_9_4_4; -.
DR Proteomes; UP000007883; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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; OmpA-like domain; 1.
DR HAMAP; MF_02204; Pal; 1.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR039001; Pal.
DR InterPro; IPR014169; Pal_lipo_C.
DR NCBIfam; TIGR02802; Pal_lipo; 1.
DR PANTHER; PTHR30329:SF22; PEPTIDOGLYCAN ASSOCIATED LIPOPROTEIN; 1.
DR PANTHER; PTHR30329; STATOR ELEMENT OF FLAGELLAR MOTOR COMPLEX; 1.
DR Pfam; PF00691; OmpA; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; OmpA-like; 1.
DR PROSITE; PS51123; OMPA_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02204};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02204}; Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_02204};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW Rule:MF_02204};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02204};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_02204};
KW Reference proteome {ECO:0000313|Proteomes:UP000007883};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02204}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..181
FT /note="Peptidoglycan-associated lipoprotein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003628278"
FT DOMAIN 67..181
FT /note="OmpA-like"
FT /evidence="ECO:0000259|PROSITE:PS51123"
FT REGION 32..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 181 AA; 19267 MW; 083CE6D7EAB2901B CRC64;
MTRFHRLPLV SALSVAAALL AACGTTTDLA DKKAPVETRQ PAADANANAN ATPQSKVATV
ELSARDAAAA AAAKARTVYF DFDSYVVKDE YKPVIDANGK FLTLDKAARL TAEGHTDERG
GREYNLALGQ KRAEAVVKAL KVMGATDGQV EAVSFGKERP ADPGHDEAAW AKNRRVELKD
K
//
