FIMV_PSEAE
ID FIMV_PSEAE Reviewed; 919 AA.
AC Q9HZA6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Motility hub protein FimV;
DE Flags: Precursor;
GN Name=fimV; OrderedLocusNames=PA3115;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK;
RX PubMed=10846211; DOI=10.1099/00221287-146-6-1321;
RA Semmler A.B., Whitchurch C.B., Leech A.J., Mattick J.S.;
RT "Identification of a novel gene, fimV, involved in twitching motility in
RT Pseudomonas aeruginosa.";
RL Microbiology 146:1321-1332(2000).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK;
RX PubMed=20345659; DOI=10.1111/j.1365-2958.2010.07135.x;
RA Fulcher N.B., Holliday P.M., Klem E., Cann M.J., Wolfgang M.C.;
RT "The Pseudomonas aeruginosa Chp chemosensory system regulates intracellular
RT cAMP levels by modulating adenylate cyclase activity.";
RL Mol. Microbiol. 76:889-904(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DOMAIN.
RX PubMed=21097635; DOI=10.1128/jb.01048-10;
RA Wehbi H., Portillo E., Harvey H., Shimkoff A.E., Scheurwater E.M.,
RA Howell P.L., Burrows L.L.;
RT "The peptidoglycan-binding protein FimV promotes assembly of the
RT Pseudomonas aeruginosa type IV pilus secretin.";
RL J. Bacteriol. 193:540-550(2011).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=21527471; DOI=10.1099/mic.0.045849-0;
RA Michel G.P.F., Aguzzi A., Ball G., Soscia C., Bleves S., Voulhoux R.;
RT "Role of fimV in type II secretion system-dependent protein secretion of
RT Pseudomonas aeruginosa on solid medium.";
RL Microbiology 157:1945-1954(2011).
RN [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=27297880; DOI=10.1128/jb.00322-16;
RA Buensuceso R.N., Nguyen Y., Zhang K., Daniel-Ivad M.,
RA Sugiman-Marangos S.N., Fleetwood A.D., Zhulin I.B., Junop M.S.,
RA Howell P.L., Burrows L.L.;
RT "The Conserved Tetratricopeptide Repeat-Containing C-Terminal Domain of
RT Pseudomonas aeruginosa FimV Is Required for Its Cyclic AMP-Dependent and
RT -Independent Functions.";
RL J. Bacteriol. 198:2263-2274(2016).
RN [7]
RP INTERACTION WITH FIML.
RX PubMed=27145134; DOI=10.1111/mmi.13410;
RA Inclan Y.F., Persat A., Greninger A., Von Dollen J., Johnson J., Krogan N.,
RA Gitai Z., Engel J.N.;
RT "A scaffold protein connects type IV pili with the Chp chemosensory system
RT to mediate activation of virulence signaling in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 101:590-605(2016).
RN [8]
RP FUNCTION.
RX PubMed=28583947; DOI=10.1128/jb.00188-17;
RA Buensuceso R.N.C., Daniel-Ivad M., Kilmury S.L.N., Leighton T.L.,
RA Harvey H., Howell P.L., Burrows L.L.;
RT "Cyclic AMP-Independent Control of Twitching Motility in Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 199:0-0(2017).
RN [9] {ECO:0007744|PDB:4MAL, ECO:0007744|PDB:4MBQ}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 862-919.
RA Daniel-Ivad M., Nguyen Y., Zhang K., Buensuceso R., Robinson H.,
RA Wolfram F., Sugiman-Marangos S.N., Junop M.S., Howell P.L., Burrows L.L.;
RT "Crystal structure of TPR2 from FimV.";
RL Submitted (AUG-2013) to the PDB data bank.
CC -!- FUNCTION: Inner membrane hub protein that plays both cAMP-dependent and
CC cAMP-independent roles in twitching motility (PubMed:27297880,
CC PubMed:28583947). Regulates intracellular cyclic AMP (cAMP) levels
CC through the activation of adenylate cyclase CyaB (PubMed:20345659).
CC Plays an essential role in a number of virulence mechanisms including
CC type IV pilus (T4P)-mediated assembly and twitching motility as well as
CC cAMP-dependent virulence gene expression (PubMed:21097635,
CC PubMed:10846211). Mediates also type II secretion (T2S) of lipases and
CC proteases (PubMed:21527471). In addition, mediates the cAMP-independent
CC localization of multiple T4P structural and regulatory components to
CC the cell poles (PubMed:21527471, PubMed:27297880, PubMed:28583947).
CC This role in directing proteins to the cell pole is not restricted to
CC type IV component and involves other proteins such as the diguanylate
CC cyclase DgcP (By similarity). {ECO:0000250|UniProtKB:A0A0H2ZC68,
CC ECO:0000269|PubMed:10846211, ECO:0000269|PubMed:20345659,
CC ECO:0000269|PubMed:21097635, ECO:0000269|PubMed:21527471,
CC ECO:0000269|PubMed:27297880, ECO:0000269|PubMed:28583947}.
CC -!- SUBUNIT: Interacts with FimL (PubMed:27145134). Interacts with DgcP (By
CC similarity). {ECO:0000250|UniProtKB:A0A0H2ZC68,
CC ECO:0000269|PubMed:27145134}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:21097635}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The N-terminal domain binds peptidoglycans through LysM motif.
CC In addition, this motif is required for PilQ stability and
CC multimerization (PubMed:21097635). The cytoplasmic domain contains
CC three discontinuous tetratricopeptide repeat (TPR) motifs involved in
CC protein-protein interactions (PubMed:27297880).
CC {ECO:0000269|PubMed:21097635, ECO:0000269|PubMed:27297880}.
CC -!- DISRUPTION PHENOTYPE: Mutants are incapable of twitching motility
CC (PubMed:10846211, PubMed:20345659). In addition, loss of FimV
CC dramatically reduces the levels of the PilQ secretin multimer through
CC which pili exit the cell (PubMed:21097635).
CC {ECO:0000269|PubMed:10846211, ECO:0000269|PubMed:20345659,
CC ECO:0000269|PubMed:21097635}.
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DR EMBL; AE004091; AAG06503.1; -; Genomic_DNA.
DR PIR; F83257; F83257.
DR RefSeq; NP_251805.1; NC_002516.2.
DR RefSeq; WP_003163304.1; NZ_QZGE01000023.1.
DR PDB; 4MAL; X-ray; 2.05 A; A/B=862-919.
DR PDB; 4MBQ; X-ray; 2.01 A; A/B/C/D/E/F=862-919.
DR PDBsum; 4MAL; -.
DR PDBsum; 4MBQ; -.
DR AlphaFoldDB; Q9HZA6; -.
DR SMR; Q9HZA6; -.
DR STRING; 287.DR97_4818; -.
DR PaxDb; Q9HZA6; -.
DR PRIDE; Q9HZA6; -.
DR EnsemblBacteria; AAG06503; AAG06503; PA3115.
DR GeneID; 879911; -.
DR KEGG; pae:PA3115; -.
DR PATRIC; fig|208964.12.peg.3267; -.
DR PseudoCAP; PA3115; -.
DR HOGENOM; CLU_007099_1_0_6; -.
DR OMA; QHSVFGA; -.
DR PhylomeDB; Q9HZA6; -.
DR BioCyc; PAER208964:G1FZ6-3171-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IMP:PseudoCAP.
DR GO; GO:0044096; C:type IV pilus; IMP:PseudoCAP.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:PseudoCAP.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 1.20.58.2200; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR038440; FimV_C_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR020011; Motility_prot_FimV_C.
DR InterPro; IPR020012; Motility_prot_FimV_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR03505; FimV_core; 1.
DR TIGRFAMs; TIGR03504; FimV_Cterm; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Coiled coil; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..919
FT /note="Motility hub protein FimV"
FT /evidence="ECO:0000255"
FT /id="PRO_5004331210"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 174..229
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118,
FT ECO:0000269|PubMed:21097635"
FT REGION 140..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 319..367
FT /evidence="ECO:0000255"
FT COMPBIAS 237..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 872..886
FT /evidence="ECO:0007829|PDB:4MBQ"
FT HELIX 889..902
FT /evidence="ECO:0007829|PDB:4MBQ"
FT HELIX 905..918
FT /evidence="ECO:0007829|PDB:4MBQ"
SQ SEQUENCE 919 AA; 96929 MW; CE6745BC3FAD414A CRC64;
MVRLRTLVRA IAAASVLTSG MAHGLGLGEI TLKSALNQPL DAEIELLEVR DLGSGEVIPS
LASPEEFSKA GVDRLYYLTD LKFTPVVKPN GKSVIRVTSS KPVQEPYLNF LVQVLWPNGR
LLREYTVLLD PPLYSPQAAA SAPQAPVSAP RATGAPRAPQ APAPVRTTAP AGSDTYRTVS
NDTLWEIAQR NRTDRVSVPQ AMLAFQELNP GAFVDGNINR LKSGQVLRIP TEQQMLERSP
REALSQVQAQ NQSWRGSRNP AAGSAGARQL DATQRNAAGS APSKVDATDN LRLVSGEGKA
SKGADKGGKG DSKAIADTLA VTKESLDSTR RENEELQSRM QDLQSQLDKL QKLIQLKDAQ
LAKLQGQLGA EGQGAAQPNA ALPDASQPNA AAQAPAQPGT PAAAAPTPAP AGEAPAAPAQ
PPVAPPPAPA AEKPPAPAVP APAPVQAAEQ PAPSFLDELL ANPLWLAVIG GSALLALLVL
LMILSRRNAQ KEKEEAQAFA ADTGEEQEDA LDLGKDGFDD LTLDEPEPQV AAVAPQVEKT
TAQTSDALGE ADIYIAYGRF NQAAELLQNA IYDEPQRTDL RLKLMEVYAE MGDREGFARQ
ENELREIGGA QPQVEQLKSR YPAMVAVAAV AGLAGAKLAQ DELDSFSLDD LSLDDSGHAA
KPDAAGQDLD DAFDLSLDDL GGDDVQADLK SDSGALDDLT LDSDLDLAAS TPADKPVDDL
DFGLDFAELA ETPSQPKHDD LGDFSLDLDA PEDKLSDDDF LLSLNDEVPA AAPADNEFTL
DTEAAEEPAL SLPDDFDLSL ADEPTEPAAP EKGEDSFAAQ LDEVSAQLDE LASNLDEPKS
ATPSFSAEDA AVASALDGDA DDDFDFLSGA DEAATKLDLA RAYIDMGDSE GARDILDEVL
AEGNDSQQAE ARELLERLA
