FIMV_PSEAB
ID FIMV_PSEAB Reviewed; 924 AA.
AC A0A0H2ZC68;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Motility hub protein FimV;
DE Flags: Precursor;
GN Name=fimV; OrderedLocusNames=PA14_23830;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP FUNCTION, INTERACTION WITH DCPG, AND SUBCELLULAR LOCATION.
RX PubMed=32080219; DOI=10.1038/s41598-020-59536-9;
RA Nicastro G.G., Kaihami G.H., Pulschen A.A., Hernandez-Montelongo J.,
RA Boechat A.L., de Oliveira Pereira T., Rosa C.G.T., Stefanello E.,
RA Colepicolo P., Bordi C., Baldini R.L.;
RT "c-di-GMP-related phenotypes are modulated by the interaction between a
RT diguanylate cyclase and a polar hub protein.";
RL Sci. Rep. 10:3077-3077(2020).
CC -!- FUNCTION: Inner membrane hub protein that plays both cAMP-dependent and
CC cAMP-independent roles in twitching motility. Regulates intracellular
CC cyclic AMP (cAMP) levels through the activation of adenylate cyclase
CC CyaB. Plays an essential role in a number of virulence mechanisms
CC including type IV pilus (T4P)-mediated assembly and twitching motility
CC as well as cAMP-dependent virulence gene expression. Mediates also type
CC II secretion (T2S) of lipases and proteases. In addition, mediates the
CC cAMP-independent localization of multiple T4P structural and regulatory
CC components to the cell poles (By similarity). This role in directing
CC proteins to the cell pole is not restricted to type IV component and
CC involves other proteins such as the diguanylate cyclase DgcP
CC (PubMed:32080219). {ECO:0000250|UniProtKB:Q9HZA6,
CC ECO:0000269|PubMed:32080219}.
CC -!- SUBUNIT: Interacts with FimL (By similarity). Interacts with DgcP
CC (PubMed:32080219). {ECO:0000250|UniProtKB:Q9HZA6,
CC ECO:0000269|PubMed:32080219}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:32080219}; 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. The cytoplasmic domain contains three discontinuous
CC tetratricopeptide repeat (TPR) motifs involved in protein-protein
CC interactions. {ECO:0000250|UniProtKB:Q9HZA6}.
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DR EMBL; CP000438; ABJ12347.1; -; Genomic_DNA.
DR RefSeq; WP_003138501.1; NZ_CP034244.1.
DR AlphaFoldDB; A0A0H2ZC68; -.
DR SMR; A0A0H2ZC68; -.
DR EnsemblBacteria; ABJ12347; ABJ12347; PA14_23830.
DR KEGG; pau:PA14_23830; -.
DR HOGENOM; CLU_007099_1_0_6; -.
DR OMA; QHSVFGA; -.
DR BioCyc; PAER208963:G1G74-1987-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Cell inner membrane; Cell membrane; Membrane; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..924
FT /note="Motility hub protein FimV"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450454"
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 REGION 140..176
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 799..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 924 AA; 97316 MW; D0A91A5D1E69A5B9 CRC64;
MVRLRTLVRA IAAASVLTSG MAHGLGLGEI TLKSALNQPL DAEIELLEVR DLGSGEVIPS
LASPEEFSKA GVDRLYYLTD LKFTPVVKPN GKSVIRVTSS KPVQEPYLNF LVQVLWPNGR
LLREYTVLLD PPLYSPQAAA SAPQAPVSAP RATGAPRTPQ APAPVRTTAP AGSDTYRTVS
NDTLWEIAQR NRTDRVSVPQ AMLAFQELNP GAFVDGNINR LKSGQVLRIP TEQQMLERSP
REALSQVQAQ NQSWRGSRNP AAGTAGARQL DATQRNAAGS APSKVDATDN LRLVSGEGKA
SKGADKGGKG DSKAIADTLA VTKESLDSTR RENEELQSRM QDLQSQLDKL QKLIQLKDAQ
LAKLQGQLGA EGQGAAQPNA ALPDASQPNA AAQAPAQPGT PAAAAPTPAP AGEAPAAPAQ
PPVAPPPAPV AEKPPAPAVP APAPVQAAEQ PAPSFLDELL ANPLWLAVIG GSALLALLVL
LMILSRRNAQ KEKEEAQAFA ADAGEEQEDA LDLGKDGFDD LTLDEPEPQV AAAAPQVEKT
TAQTSDALGE ADIYIAYGRF NQAAELLQNA IYDEPQRTDL RLKLMEVYAE MGDREGFARQ
ENELREIGGA QPQVEQLKSR YPAMVAVAAV AGLAGAKLAQ DELDSFSLDD LSLDDSGHAA
KPDAAGQDLD DAFDLSLDDL GGGDLGSDDV QADLKSDSGA LDDLTLDSDL DLAASTAADK
PVDDLDFGLD FAELAETPSQ PKHDDLGDFS LDLDAPEDKL SDDDFLLSLN DEVPAAAPAN
NEFTLDTEAA EEPALSLPDD FDLSLADEPT EPAAPEKGED SFAAQLDEVS AQLDELASNL
DEPKSAAPSF SAEDAAVASA LDGDADDDFD FLSGADEAAT KLDLARAYID MGDSEGARDI
LDEVLAEGND SQQAEARELL ERLA
