HAP2_HAEIF
ID HAP2_HAEIF Reviewed; 1394 AA.
AC P45387;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Adhesion and penetration protein autotransporter;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Adhesion and penetration protein;
DE Contains:
DE RecName: Full=Adhesion and penetration protein translocator;
DE Flags: Precursor;
GN Name=hap;
OS Haemophilus influenzae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NTHi N187;
RX PubMed=7830568; DOI=10.1111/j.1365-2958.1994.tb01283.x;
RA St Geme J.W. III, de la Morena M.L., Falkow S.;
RT "A Haemophilus influenzae IgA protease-like protein promotes intimate
RT interaction with human epithelial cells.";
RL Mol. Microbiol. 14:217-233(1994).
CC -!- FUNCTION: Probable protease; promotes adherence and invasion by
CC directly binding to a host cell structure.
CC -!- INTERACTION:
CC P45387; P45387: hap; NbExp=2; IntAct=EBI-7074441, EBI-7074441;
CC -!- SUBCELLULAR LOCATION: [Adhesion and penetration protein
CC autotransporter]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Adhesion and penetration protein]: Secreted.
CC Cell surface.
CC -!- SUBCELLULAR LOCATION: [Adhesion and penetration protein translocator]:
CC Cell outer membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter
CC domain) is localized in the outer membrane. {ECO:0000250}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface, with subsequent cleavage (By similarity).
CC {ECO:0000250}.
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DR EMBL; U11024; AAB03707.1; -; Genomic_DNA.
DR PIR; S60762; S60762.
DR PDB; 3SYJ; X-ray; 2.20 A; A=26-1036.
DR PDBsum; 3SYJ; -.
DR AlphaFoldDB; P45387; -.
DR SMR; P45387; -.
DR MINT; P45387; -.
DR MEROPS; S06.006; -.
DR TCDB; 1.B.12.3.2; the autotransporter-1 (at-1) family.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.20; -; 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.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR InterPro; IPR004899; Pertactin_central.
DR Pfam; PF02395; Peptidase_S6; 2.
DR Pfam; PF03212; Pertactin; 1.
DR PRINTS; PR00921; IGASERPTASE.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell outer membrane; Hydrolase; Membrane;
KW Periplasm; Protease; Secreted; Serine protease; Signal; Transmembrane;
KW Transmembrane beta strand; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1394
FT /note="Adhesion and penetration protein autotransporter"
FT /id="PRO_0000387596"
FT CHAIN 26..?
FT /note="Adhesion and penetration protein"
FT /id="PRO_0000026956"
FT CHAIN ?..1394
FT /note="Adhesion and penetration protein translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026957"
FT DOMAIN 26..286
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1140..1394
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 848..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 243
FT /evidence="ECO:0000250"
FT CONFLICT 1167
FT /note="Missing (in Ref. 1; AAB03707)"
FT /evidence="ECO:0000305"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:3SYJ"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:3SYJ"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 312..333
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 428..439
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 448..458
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 474..489
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 592..595
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 602..607
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 628..634
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 650..659
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 661..666
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 668..679
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 684..687
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 693..700
FT /evidence="ECO:0007829|PDB:3SYJ"
FT TURN 702..704
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 707..713
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 717..722
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 739..748
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 759..763
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 767..770
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 779..789
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 798..803
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 810..812
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 817..822
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 831..845
FT /evidence="ECO:0007829|PDB:3SYJ"
FT HELIX 847..849
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 877..880
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 884..895
FT /evidence="ECO:0007829|PDB:3SYJ"
FT TURN 896..899
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 903..906
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 912..920
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 931..940
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 946..950
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 955..957
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 960..967
FT /evidence="ECO:0007829|PDB:3SYJ"
FT STRAND 970..974
FT /evidence="ECO:0007829|PDB:3SYJ"
SQ SEQUENCE 1394 AA; 155441 MW; 5BF28660103F60F9 CRC64;
MKKTVFRLNF LTACISLGIV SQAWAGHTYF GIDYQYYRDF AENKGKFTVG AQNIKVYNKQ
GQLVGTSMTK APMIDFSVVS RNGVAALVEN QYIVSVAHNV GYTDVDFGAE GNNPDQHRFT
YKIVKRNNYK KDNLHPYEDD YHNPRLHKFV TEAAPIDMTS NMNGSTYSDR TKYPERVRIG
SGRQFWRNDQ DKGDQVAGAY HYLTAGNTHN QRGAGNGYSY LGGDVRKAGE YGPLPIAGSK
GDSGSPMFIY DAEKQKWLIN GILREGNPFE GKENGFQLVR KSYFDEIFER DLHTSLYTRA
GNGVYTISGN DNGQGSITQK SGIPSEIKIT LANMSLPLKE KDKVHNPRYD GPNIYSPRLN
NGETLYFMDQ KQGSLIFASD INQGAGGLYF EGNFTVSPNS NQTWQGAGIH VSENSTVTWK
VNGVEHDRLS KIGKGTLHVQ AKGENKGSIS VGDGKVILEQ QADDQGNKQA FSEIGLVSGR
GTVQLNDDKQ FDTDKFYFGF RGGRLDLNGH SLTFKRIQNT DEGAMIVNHN TTQAANVTIT
GNESIVLPNG NNINKLDYRK EIAYNGWFGE TDKNKHNGRL NLIYKPTTED RTLLLSGGTN
LKGDITQTKG KLFFSGRPTP HAYNHLNKRW SEMEGIPQGE IVWDHDWINR TFKAENFQIK
GGSAVVSRNV SSIEGNWTVS NNANATFGVV PNQQNTICTR SDWTGLTTCQ KVDLTDTKVI
NSIPKTQING SINLTDNATA NVKGLAKLNG NVTLTNHSQF TLSNNATQIG NIRLSDNSTA
TVDNANLNGN VHLTDSAQFS LKNSHFSHQI QGDKGTTVTL ENATWTMPSD TTLQNLTLNN
STITLNSAYS ASSNNTPRRR SLETETTPTS AEHRFNTLTV NGKLSGQGTF QFTSSLFGYK
SDKLKLSNDA EGDYILSVRN TGKEPETLEQ LTLVESKDNQ PLSDKLKFTL ENDHVDAGAL
RYKLVKNDGE FRLHNPIKEQ ELHNDLVRAE QAERTLEAKQ VEPTAKTQTG EPKVRSRRAA
RAAFPDTLPD QSLLNALEAK QAELTAETQK SKAKTKKVRS KRAVFSDPLL DQSLFALEAA
LEVIDAPQQS EKDRLAQEEA EKQRKQKDLI SRYSNSALSE LSATVNSMLS VQDELDRLFV
DQAQSAVWTN IAQDKRRYDS DAFRAYQQQK TNLRQIGVQK ALANGRIGAV FSHSRSDNTF
DEQVKNHATL TMMSGFAQYQ WGDLQFGVNV GTGISASKMA EEQSRKIHRK AINYGVNASY
QFRLGQLGIQ PYFGVNRYFI ERENYQSEEV RVKTPSLAFN RYNAGIRVDY TFTPTDNISV
KPYFFVNYVD VSNANVQTTV NLTVLQQPFG RYWQKEVGLK AEILHFQISA FISKSQGSQL
GKQQNVGVKL GYRW
