ID   PILQ_NEIMA              Reviewed;         761 AA.
AC   Q9JVW4; A1IQ85;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Type IV pilus biogenesis and competence protein PilQ;
DE   Flags: Precursor;
GN   Name=pilQ; OrderedLocusNames=NMA0650;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
CC   -!- FUNCTION: Required for type IV pilus biogenesis and competence. Could
CC       function as a pore for exit of the pilus but also as a channel for
CC       entry of heme and antimicrobial agents and uptake of transforming DNA
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homododecamer. Tetramer of trimer (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial secretin family. PilQ subfamily.
CC       {ECO:0000305}.
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; AL157959; CAM07913.1; -; Genomic_DNA.
DR   PIR; A81985; A81985.
DR   RefSeq; WP_002219789.1; NC_003116.1.
DR   PDB; 4AR0; NMR; -; A=335-434.
DR   PDBsum; 4AR0; -.
DR   AlphaFoldDB; Q9JVW4; -.
DR   SMR; Q9JVW4; -.
DR   EnsemblBacteria; CAM07913; CAM07913; NMA0650.
DR   GeneID; 61280695; -.
DR   KEGG; nma:NMA0650; -.
DR   HOGENOM; CLU_006756_0_1_4; -.
DR   OMA; QNVPWDQ; -.
DR   BioCyc; NMEN122587:NMA_RS03285-MON; -.
DR   Proteomes; UP000000626; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   Gene3D; 3.30.1370.120; -; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR001775; GspD/PilQ.
DR   InterPro; IPR005644; NolW-like.
DR   InterPro; IPR038591; NolW-like_sf.
DR   InterPro; IPR013355; Pilus_4_PilQ.
DR   InterPro; IPR011662; Secretin/TonB_short_N.
DR   InterPro; IPR004846; T2SS/T3SS.
DR   InterPro; IPR004845; T2SS_GspD_CS.
DR   Pfam; PF11741; AMIN; 1.
DR   Pfam; PF00263; Secretin; 1.
DR   Pfam; PF03958; Secretin_N; 1.
DR   Pfam; PF07660; STN; 1.
DR   PRINTS; PR00811; BCTERIALGSPD.
DR   SMART; SM00965; STN; 1.
DR   TIGRFAMs; TIGR02515; IV_pilus_PilQ; 1.
DR   PROSITE; PS00875; T2SP_D; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell outer membrane; Competence; Membrane; Protein transport;
KW   Signal; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..761
FT                   /note="Type IV pilus biogenesis and competence protein
FT                   PilQ"
FT                   /id="PRO_0000013116"
FT   REGION          135..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          339..348
FT                   /evidence="ECO:0007829|PDB:4AR0"
FT   HELIX           349..358
FT                   /evidence="ECO:0007829|PDB:4AR0"
FT   STRAND          363..366
FT                   /evidence="ECO:0007829|PDB:4AR0"
FT   STRAND          373..382
FT                   /evidence="ECO:0007829|PDB:4AR0"
FT   HELIX           383..393
FT                   /evidence="ECO:0007829|PDB:4AR0"
FT   STRAND          396..401
FT                   /evidence="ECO:0007829|PDB:4AR0"
FT   STRAND          404..409
FT                   /evidence="ECO:0007829|PDB:4AR0"
FT   HELIX           410..418
FT                   /evidence="ECO:0007829|PDB:4AR0"
FT   STRAND          425..427
FT                   /evidence="ECO:0007829|PDB:4AR0"
SQ   SEQUENCE   761 AA;  81786 MW;  F551769291E07BD5 CRC64;
     MNTKLTKIIS GLFVATAAFQ TASAGNITDI KVSSLPNKQK IVKVSFDKEI VNPTGFVTSS
     PARIALDFEQ TGISMDQQVL EYADPLLSKI SAAQNSSRAR LVLNLNKPGQ YNTEVRGNKV
     WIFINESDDT VSAPARPAVK AAPAAPAKQQ AAAPSTKSAV SVSKPFTPAK QQAAAPFTES
     VVSVSAPFSP AKQQAAASAK QQTAAPAKQQ AATPAKQTNI DFRKDGKNAG IIELAALGFA
     GQPDISQQHD HIIVTLKNHT LPTTLQRSLD VADFKTPVQK VTLKRLNNDT QLIITTAGNW
     ELVNKSAAPG YFTFQVLPKK QNLESGGVNN APKTFTGRKI SLDFQDVEIR TILQILAKES
     GMNIVASDSV NGKMTLSLKD VPWDQALDLV MQARNLDMRQ QGNIVNIAPR DELLAKDKAF
     LQAEKDIADL GALYSQNFQL KYKNVEEFRS ILRLDNADTT GNRNTLVSGR GSVLIDPATN
     TLIVTDTRSV IEKFRKLIDE LDVPAQQVMI EARIVEAADG FSRDLGVKFG ATGKKKLKND
     TSAFGWGVNS GFGGDDKWGA ETKINLPITA AANSISLVRA ISSGALNLEL SASESLSKTK
     TLANPRVLTQ NRKEAKIESG YEIPFTVTSI ANGGSSTNTE LKKAVLGLTV TPNITPDGQI
     IMTVKINKDS PAQCASGNQT ILCISTKNLN TQAMVENGGT LIVGGIYEED NGNTLTKVPL
     LGDIPVIGNL FKTRGKKTDR RELLIFITPR IMGTAGNSLR Y