ID A0A328B9J7_9CAUL Unreviewed; 177 AA.
AC A0A328B9J7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:RAK63121.1};
GN ORFNames=DJ019_17800 {ECO:0000313|EMBL:RAK63121.1};
OS Phenylobacterium kunshanense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1445034 {ECO:0000313|EMBL:RAK63121.1, ECO:0000313|Proteomes:UP000249524};
RN [1] {ECO:0000313|EMBL:RAK63121.1, ECO:0000313|Proteomes:UP000249524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUT-10 {ECO:0000313|EMBL:RAK63121.1,
RC ECO:0000313|Proteomes:UP000249524};
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA Winkler M.E.;
RL Submitted (MAY-2018) 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 -!- 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}.
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:RAK63121.1}.
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DR EMBL; QFYS01000009; RAK63121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328B9J7; -.
DR OrthoDB; 9809164at2; -.
DR Proteomes; UP000249524; Unassembled WGS sequence.
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; 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.
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};
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW 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:UP000249524};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02204}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..177
FT /note="Peptidoglycan-associated lipoprotein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016319241"
FT DOMAIN 58..175
FT /note="OmpA-like"
FT /evidence="ECO:0000259|PROSITE:PS51123"
FT REGION 25..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 177 AA; 18464 MW; 4F883ED7B20CA41B CRC64;
MMRATRTLIL AAAASALLAG CASKPKPALT AAPPSSEPGP STELPPPPAA GAVSQSAQEA
LAATAGDRVY FDFDSSALDA EDRETLRRQA AWLAANPGVQ ARVEGHADER GTREYNLALG
ARRASAARQA LIEGGVAATR ITTISYGKER PLDPASNEEA WARNRNAYTV VIEAGRP
//