ID A0A1G7QDP3_9GAMM Unreviewed; 179 AA.
AC A0A1G7QDP3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Peptidoglycan-associated protein {ECO:0000256|HAMAP-Rule:MF_02204};
GN Name=pal {ECO:0000256|HAMAP-Rule:MF_02204};
GN ORFNames=SAMN05216571_103217 {ECO:0000313|EMBL:SDF96636.1};
OS Halomonas taeanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=284577 {ECO:0000313|EMBL:SDF96636.1, ECO:0000313|Proteomes:UP000198641};
RN [1] {ECO:0000313|EMBL:SDF96636.1, ECO:0000313|Proteomes:UP000198641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH539 {ECO:0000313|EMBL:SDF96636.1,
RC ECO:0000313|Proteomes:UP000198641};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the Pal lipoprotein family. {ECO:0000256|HAMAP-
CC Rule:MF_02204}.
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DR EMBL; FNCI01000003; SDF96636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7QDP3; -.
DR STRING; 284577.SAMN05216571_103217; -.
DR OrthoDB; 9809164at2; -.
DR Proteomes; UP000198641; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-KW.
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; IPR006690; OMPA-like_CS.
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; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 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|ARBA:ARBA00023237};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000313|EMBL:SDF96636.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00473}; Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000198641};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..179
FT /note="Peptidoglycan-associated protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011483727"
FT DOMAIN 66..179
FT /note="OmpA-like"
FT /evidence="ECO:0000259|PROSITE:PS51123"
FT REGION 27..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 179 AA; 19327 MW; 97EDE9A1DD502A22 CRC64;
MHLFPYAKHL AVAVSLVVMA GCSSTGGTQD GSMAGSEGAG STNGGASSQG MNSGQVGSNS
MGMRDGQQDG IPQVRTIYFD YDRDTIRSEF EPVMAAHAQY LRSHPNANVI LQGHTDERGT
REYNLALGER RANAVQRFLM VQGVSPSQLE VVSYGEERPA VRGSSEDSYA QNRRVVFDY
//
