ID   Q9X7H1_NEIMI            Unreviewed;      1457 AA.
AC   Q9X7H1;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 2.
DT   24-JAN-2024, entry version 95.
DE   SubName: Full=App protein {ECO:0000313|EMBL:CAB43832.2};
GN   Name=app {ECO:0000313|EMBL:CAB43832.2};
OS   Neisseria meningitidis serogroup B.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=491 {ECO:0000313|EMBL:CAB43832.2};
RN   [1] {ECO:0000313|EMBL:CAB43832.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B:15:P1.16 {ECO:0000313|EMBL:CAB43832.2};
RX   PubMed=11532129; DOI=10.1046/j.1365-2958.2001.02516.x;
RA   Abdel Hadi H., Wooldridge K.G., Robinson K., Ala Aldeen D.A.;
RT   "Identification and characterization of App: an immunogenic autotransporter
RT   protein of Neisseria meningitidis.";
RL   Mol. Microbiol. 41:611-623(2001).
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000256|ARBA:ARBA00004571}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004571}. Cell surface
CC       {ECO:0000256|ARBA:ARBA00004241}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Periplasm
CC       {ECO:0000256|ARBA:ARBA00004418}. Secreted
CC       {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; AJ242535; CAB43832.2; -; Genomic_DNA.
DR   MEROPS; S06.006; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01343; PL1_Passenger_AT; 1.
DR   Gene3D; 2.160.20.20; -; 2.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR005546; Autotransporte_beta.
DR   InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR   InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR   InterPro; IPR006315; OM_autotransptr_brl_dom.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR000710; Peptidase_S6.
DR   InterPro; IPR030396; Peptidase_S6_dom.
DR   InterPro; IPR004899; Pertactin_central.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   NCBIfam; TIGR01414; autotrans_barl; 1.
DR   PANTHER; PTHR12338:SF10; ADHESION AND PENETRATION PROTEIN AUTOTRANSPORTER; 1.
DR   PANTHER; PTHR12338; AUTOTRANSPORTER; 1.
DR   Pfam; PF02395; Peptidase_S6; 2.
DR   Pfam; PF03212; Pertactin; 1.
DR   PRINTS; PR00921; IGASERPTASE.
DR   SMART; SM00869; Autotransporter; 1.
DR   SUPFAM; SSF103515; Autotransporter; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR   PROSITE; PS51691; PEPTIDASE_S6; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          43..310
FT                   /note="Peptidase S6"
FT                   /evidence="ECO:0000259|PROSITE:PS51691"
FT   DOMAIN          1204..1457
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000259|PROSITE:PS51208"
FT   REGION          921..948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1135..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1457 AA;  159957 MW;  CE62390B6C04B781 CRC64;
     MKTTDKRTTE THRKAPKTGR IRFSPAYLAI CLSFGILPQA WAGHTYFGIN YQYYRDFAEN
     KGKFAVGAKD IEVYNKKGEL VGKSMTKAPM IDFSVVSRNG VAALVGDQYI VSVAHNGGYN
     NVDFGAEGRN PDQHRFTYKI VKRNNYKAGT KGHPYGGDYH MPRLHKFVTD AEPVEMTSYM
     DGRKYIDQNN YPDRVRIGAG RQYWRSDEDE PNNRESSYHI ASAYSWLVGG NTFAQNGSGG
     GTVNLGSEKI KHSPYGFLPT GGSFGDSGSP MFIYDAQKQK WLINGVLQTG NPYIGKSNGF
     QLVRKDWFYD EIFAGDAHSV FYEPRQNGKY SFNDDNNGTG KINAKHEHNS LPNRLKTRTV
     QLFNVSLSET AREPVYHAAG GVNSYRPRLN NGENISFIDE GKGELILTSN INQGAGGLYF
     QGDFTVSPEN NETWQGAGVH ISEDSTVTWK VNGVANDRLS KIGKGTLHVQ AKGENQGSIS
     VGDGTVILDQ QADDKGKKQA FSEIGLVSGR GTVQLNADNQ FNPDKLYFGF RGGRLDLNGH
     SLSFHRIQNT DEGAMIVNHN QDKESTVTIT GNKDIATTGN NNSLDSKKEI AYNGWFGEKD
     TTKTNGRLNL VYQPAAEDRT LLLSGGTNLN GNITQTNGKL FFSGRPTPHA YNHLNDHWSQ
     KEGIPRGEIV WDNDWINRTF KAENFQIKGG QAVVSRNVAK VKGDWHLSNH AQAVFGVAPH
     QSHTICTRSD WTGLTNCVEK TITDDKVIAS LTKTDISGNV DLADHAHLNL TGLATLNGSL
     SANGDTRYTV SHYATQNGNL SLVGNAQATF NQATLNGNTS ASGNASFNLS DHAVQNGSLT
     LSGNAKANVS HSALNGNVSL ADKAVFHFES SRFTGQISGG KDTALHLKDS EWTLPSGTEL
     GNLNLDNATI TLNSAYRHNA AGAQTGSATD APRRRSRRSR RSLLSVTPPT SVESRFNTLT
     VNGKLNGQGT FRFMSELFGY RSDKLKLAES SEGTYTLAVN NTGNEPASLE QLTVVEGKDN
     KPLSENLNFT LQNEHVDAGA WRYQLIRKDG EFRLHNPVKE QELSDKLGKA EAKKQAEKDN
     AQSLDALIAA GRDAVEKTES VAEPARQAGG ENVGIMQAEE EKKRVQADKD TALAKQREAE
     TRPATTAFPR ARRARRDLPQ LQPQPQPQPQ RDLISRYANS GLSEFSATLN SVFAVQDELD
     RVFAEDRRNA VWTSGIRDTK HYRSQDFRAY RQQTDLRQIG MQKNLGSGRV GILFSHNRTE
     NTFDDGIGNS ARLAHGAVFG QYGIDRFYIG ISAGAGFSSG SLSDGIGGKI RRRVLHYGIQ
     ARYRAGFGGF GIEPHIGATR YFVQKADYRY ENVNIATPGL AFNRYRAGIK ADYSFKPAQH
     ISITPYLSLS YTDAASGKVR TRVNTAVLAQ DFGKTRSAEW GVNAEIKGFT LSLHAAAAKG
     PQLEAQHSAG IKLGYRW
//