ID F9R7W9_VIBSN Unreviewed; 439 AA.
AC F9R7W9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Tol-Pal system protein TolB {ECO:0000256|HAMAP-Rule:MF_00671};
GN Name=tolB {ECO:0000256|HAMAP-Rule:MF_00671,
GN ECO:0000313|EMBL:EGU36524.1};
GN ORFNames=VIBRN418_07326 {ECO:0000313|EMBL:EGU36524.1};
OS Vibrio sp. (strain N418).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU36524.1, ECO:0000313|Proteomes:UP000003627};
RN [1] {ECO:0000313|EMBL:EGU36524.1, ECO:0000313|Proteomes:UP000003627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N418 {ECO:0000313|EMBL:EGU36524.1,
RC ECO:0000313|Proteomes:UP000003627};
RA Strain E.A., Brown E., Allard M.W.;
RL Submitted (AUG-2011) 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_00671}.
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_00671}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|HAMAP-Rule:MF_00671}.
CC -!- SIMILARITY: Belongs to the TolB family. {ECO:0000256|ARBA:ARBA00009820,
CC ECO:0000256|HAMAP-Rule:MF_00671}.
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:EGU36524.1}.
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DR EMBL; AFWD01000016; EGU36524.1; -; Genomic_DNA.
DR AlphaFoldDB; F9R7W9; -.
DR eggNOG; COG0823; Bacteria.
DR Proteomes; UP000003627; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0017038; P:protein import; IEA:InterPro.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 3.40.50.10070; TolB, N-terminal domain; 1.
DR HAMAP; MF_00671; TolB; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR014167; Tol-Pal_TolB.
DR InterPro; IPR007195; TolB_N.
DR NCBIfam; TIGR02800; propeller_TolB; 1.
DR PANTHER; PTHR36842; PROTEIN TOLB HOMOLOG; 1.
DR PANTHER; PTHR36842:SF1; TOL-PAL SYSTEM PROTEIN TOLB; 1.
DR Pfam; PF07676; PD40; 3.
DR Pfam; PF04052; TolB_N; 1.
DR SUPFAM; SSF52964; TolB, N-terminal domain; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00671};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00671};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_00671};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00671}.
FT DOMAIN 13..115
FT /note="TolB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04052"
SQ SEQUENCE 439 AA; 48559 MW; 13D7C0ED96BDE0ED CRC64;
MIASSVQFAN AALELVITDG IDSARPIAIV PFKWEGAKPL PQDVSAVIAS DLQRSGKFSP
VPTSKMPQTP YNESEVNFDA WTRLGVDSLL TGSITQDAKG DYVINYQLVD VVRGQLTQGQ
SKALGEDGEL VLSKDHVLFN KRATVPESRL REYAHRISDL VYEQLTGERG AFLTRIAYVV
VNDKESYPYQ LRVADYDGYN ERLVLRSKQP LMSPSWSPDG KKLAYVSFQN GQAEIYMMDI
YTGEREKLTS YPRHNGAPKF SPDGKTLALV LSKTGSLQVY TMDIKTRKLT QITRGRSNNT
EPFWHPDGKS LIFTSDRGGK PQIYQVNLAG GDTSRITWQG SQNLGGQITP DGRFLVMVNR
SNTGFNLAKQ DLETGAVQVL TKTLLDESPS IAPNGGMVIY SSIYNKTNVL SMVSIDGRFK
ARLPATNGRV RAPAWSPFL
//