PILM_PSEAE
ID PILM_PSEAE Reviewed; 354 AA.
AC G3XD28;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Type IV pilus inner membrane component PilM {ECO:0000303|PubMed:19857645};
GN Name=pilM; OrderedLocusNames=PA5044;
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, SUBCELLULAR LOCATION, INTERACTION WITH PILN; PILO AND PILP, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19857645; DOI=10.1016/j.jmb.2009.09.034;
RA Ayers M., Sampaleanu L.M., Tammam S., Koo J., Harvey H., Howell P.L.,
RA Burrows L.L.;
RT "PilM/N/O/P proteins form an inner membrane complex that affects the
RT stability of the Pseudomonas aeruginosa type IV pilus secretin.";
RL J. Mol. Biol. 394:128-142(2009).
RN [3]
RP INTERACTION WITH PILN.
RX PubMed=19857646; DOI=10.1016/j.jmb.2009.09.037;
RA Sampaleanu L.M., Bonanno J.B., Ayers M., Koo J., Tammam S., Burley S.K.,
RA Almo S.C., Burrows L.L., Howell P.L.;
RT "Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable
RT heterodimeric complex.";
RL J. Mol. Biol. 394:143-159(2009).
RN [4] {ECO:0007744|PDB:5EOU, ECO:0007744|PDB:5EOX, ECO:0007744|PDB:5EOY}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ATP AND MAGNESIUM,
RP AND INTERACTION WITH PILN; PILB; PILC AND PILT.
RX PubMed=27022027; DOI=10.1074/jbc.m116.718353;
RA McCallum M., Tammam S., Little D.J., Robinson H., Koo J., Shah M.,
RA Calmettes C., Moraes T.F., Burrows L.L., Howell P.L.;
RT "PilN Binding Modulates the Structure and Binding Partners of the
RT Pseudomonas aeruginosa Type IVa Pilus Protein PilM.";
RL J. Biol. Chem. 291:11003-11015(2016).
CC -!- FUNCTION: Inner membrane component of the type IV (T4S) secretion
CC system that plays a role in surface and host cell adhesion,
CC colonization, biofilm maturation, virulence, and twitching, a form of
CC surface-associated motility. PilN/PilO heterodimers form the foundation
CC of the inner-membrane PilM/PilN/PilO/PilP complex which plays an
CC essential role in the assembly of a functional T4 pilus
CC (PubMed:19857645, PubMed:19857646). In turn, associates with PilN and
CC facilitates PilM functionally relevant structural changes that
CC differentially impacts PilM binding to PilB, PilT, and PilC
CC (PubMed:27022027). {ECO:0000269|PubMed:19857645,
CC ECO:0000269|PubMed:19857646, ECO:0000269|PubMed:27022027}.
CC -!- SUBUNIT: Interacts with PilN; this interaction modulates PilM ATP
CC binding site (PubMed:19857645, PubMed:19857646, PubMed:27022027).
CC Interacts with PilP (PubMed:19857645). Interacts with PilO
CC (PubMed:19857645). Interacts with PilB, PilC and PilT
CC (PubMed:27022027). {ECO:0000269|PubMed:19857645,
CC ECO:0000269|PubMed:19857646, ECO:0000269|PubMed:27022027}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19857645}.
CC Note=Localizes to the inner membrane through interaction with PilN.
CC {ECO:0000269|PubMed:19857645}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants lack surface pili.
CC {ECO:0000269|PubMed:19857645}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG08429.1; -; Genomic_DNA.
DR PIR; S77726; S77726.
DR RefSeq; NP_253731.1; NC_002516.2.
DR RefSeq; WP_003110888.1; NZ_QZGE01000002.1.
DR PDB; 5EOU; X-ray; 2.40 A; A/B=1-354.
DR PDB; 5EOX; X-ray; 2.40 A; A/B=1-354.
DR PDB; 5EOY; X-ray; 2.50 A; A/B=1-354.
DR PDB; 5EQ6; X-ray; 3.50 A; A/B=1-354.
DR PDBsum; 5EOU; -.
DR PDBsum; 5EOX; -.
DR PDBsum; 5EOY; -.
DR PDBsum; 5EQ6; -.
DR AlphaFoldDB; G3XD28; -.
DR SMR; G3XD28; -.
DR STRING; 287.DR97_2399; -.
DR PaxDb; G3XD28; -.
DR PRIDE; G3XD28; -.
DR DNASU; 881162; -.
DR EnsemblBacteria; AAG08429; AAG08429; PA5044.
DR GeneID; 881162; -.
DR KEGG; pae:PA5044; -.
DR PATRIC; fig|208964.12.peg.5288; -.
DR PseudoCAP; PA5044; -.
DR HOGENOM; CLU_050686_1_0_6; -.
DR InParanoid; G3XD28; -.
DR OMA; EKVQDRQ; -.
DR PhylomeDB; G3XD28; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044096; C:type IV pilus; IMP:PseudoCAP.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0043683; P:type IV pilus assembly; IMP:PseudoCAP.
DR GO; GO:0043107; P:type IV pilus-dependent motility; IMP:PseudoCAP.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR005883; PilM.
DR InterPro; IPR003494; SHS2_FtsA.
DR Pfam; PF11104; PilM_2; 1.
DR PIRSF; PIRSF019169; PilM; 1.
DR SMART; SM00842; FtsA; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01175; pilM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..354
FT /note="Type IV pilus inner membrane component PilM"
FT /id="PRO_0000450556"
FT BINDING 18..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27022027,
FT ECO:0007744|PDB:5EOU"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27022027,
FT ECO:0007744|PDB:5EOY"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27022027,
FT ECO:0007744|PDB:5EOY"
FT BINDING 202..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27022027,
FT ECO:0007744|PDB:5EOU"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27022027,
FT ECO:0007744|PDB:5EOU"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27022027,
FT ECO:0007744|PDB:5EOU"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 19..32
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5EOX"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:5EOU"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5EOU"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:5EOU"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 261..280
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:5EQ6"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:5EOU"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:5EOU"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:5EOU"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5EOU"
SQ SEQUENCE 354 AA; 37983 MW; 731B77EB77BCBD50 CRC64;
MLGLIKKKAN TLLGIDISST SVKLLELSRS GGRYKVEAYA VEPLPPNAVV EKNIVELEGV
GQALSRVLVK AKTNLKSAVV AVAGSAVITK TIEMEAGLSE DELENQLKIE ADQYIPYPLE
EVAIDFEVQG LSARNPERVD VLLAACRKEN VEVREAALAL AGLTAKVVDV EAYALERSYA
LLSSQLGADT DQLTVAVVDI GATMTTLSVL HNGRTIYTRE QLFGGRQLTE EIQRRYGLSV
EEAGLAKKQG GLPDDYDSEV LRPFKDAVVQ QVSRSLQFFF AAGQFNDVDY IVLAGGTASI
QDLDRLIQQK IGTPTLVANP FADMALNGKV NAGALASDAP ALMIACGLAL RSFD
