HAP1_HAEIN
ID HAP1_HAEIN Reviewed; 1409 AA.
AC P44596;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
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 AltName: Full=Helper peptide;
DE Flags: Precursor;
GN Name=hap; OrderedLocusNames=HI_0248;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Probable protease; promotes adherence and invasion by
CC directly binding to a host cell structure. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Adhesion and penetration protein
CC autotransporter]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Adhesion and penetration protein]: Secreted
CC {ECO:0000305}. Cell surface {ECO:0000305}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=L42023; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64057; C64057.
DR AlphaFoldDB; P44596; -.
DR SMR; P44596; -.
DR MEROPS; S06.006; -.
DR PRIDE; P44596; -.
DR Proteomes; UP000000579; Chromosome.
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: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 Gene3D; 2.40.128.130; -; 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; 1.
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 3: Inferred from homology;
KW Cell adhesion; Cell outer membrane; Hydrolase; Membrane; Periplasm;
KW Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Transmembrane; Transmembrane beta strand; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1409
FT /note="Adhesion and penetration protein autotransporter"
FT /id="PRO_0000387595"
FT CHAIN 26..?
FT /note="Adhesion and penetration protein"
FT /id="PRO_0000026954"
FT CHAIN ?..1409
FT /note="Adhesion and penetration protein translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026955"
FT DOMAIN 26..294
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1156..1409
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 866..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /evidence="ECO:0000250"
SQ SEQUENCE 1409 AA; 156815 MW; F51C219C312A146E CRC64;
MKKTVFRLNF LTACVSLGIA SQAWAGHTYF GIDYQYYRDF AENKGKFTVG AKNIEVYNKE
GQLVGTSMTK APMIDFSVVS RNGVAALVGD QYIVSVAHNG GYNDVDFGAE GRNPDQHRFT
YQIVKRNNYQ AWERKHPYDG DYHMPRLHKF VTEAEPVGMT TNMDGKVYAD RENYPERVRI
GSGRQYWRTD KDEETNVHSS YYVSGAYRYL TAGNTHTQSG NGNGTVNLSG NVVSPNHYGP
LPTGGSKGDS GSPMFIYDAK KKQWLINAVL QTGHPFFGRG NGFQLIREEW FYNEVLAVDT
PSVFQRYIPP INGHYSFVSN NDGTGKLTLT RPSKDGSKAK SEVGTVKLFN PSLNQTAKEH
VKAAAGYNIY QPRMEYGKNI YLGDQGKGTL TIENNINQGA GGLYFEGNFV VKGKQNNITW
QGAGVSIGQD ATVEWKVHNP ENDRLSKIGI GTLLVNGKGK NLGSLSAGNG KVILDQQADE
AGQKQAFKEV GIVSGRATVQ LNSTDQVDPN NIYFGFRGGR LDLNGHSLTF KRIQNTDEGA
MIVNHNTTQV ANITITGNES ITAPSNKKNI NKLDYSKEIA YNGWFGETDK NKHNGRLNLI
YKPTTEDRTL LLSGGTNLKG DITQTKGKLF FSGRPTPHAY NHLDKRWSEM EGIPQGEIVW
DYDWINRTFK AENFQIKGGS AVVSRNVSSI EGNWTVSNNA NATFGVVPNQ QNTICTRSDW
TGLTTCKTVN LTDTKVINSI PITQINGSIN LTNNATVNIH GLAKLNGNVT LIDHSQFTLS
NNATQTGNIK LSNHANATVN NATLNGNVHL TDSAQFSLKN SHFWHQIQGD KDTTVTLENA
TWTMPSDTTL QNLTLNNSTV TLNSAYSASS NNAPRHRRSL ETETTPTSAE HRFNTLTVNG
KLSGQGTFQF TSSLFGYKSD KLKLSNDAEG DYTLSVRNTG KEPVTLEQLT LIESLDNKPL
SDKLKFTLEN DHVDAGALRY KLVKNKGEFR LHNPIKEQEL LNDLVRAEQA EQTLEAKQVE
QTAEKQKSKA KARSRRAVLS DTPSAQSLLN ALEAKQVEQT TETQTSKPKT KKGRSKRALS
AAFSDTPFDL SQLKVFEVKL EVINAQPQVK KEPQDQEEQG KQKELISRYS NSALSELSAT
VNSMFSVQDE LDRLFVDQAQ SALWTNIAQD KRRYDSDAFR AYQQKTNLRQ IGVQKALDNG
RIGAVFSHSR SDNTFDEQVK NHATLTMMSG FAQYQWGDLQ FGVNVGAGIS ASKMAEEQSR
KIHRKAINYG VNASYQFRLG QLGIQPYLGV NRYFIERENY QSEEVKVQTP SLAFNRYNAG
IRVDYTFTPT NNISVKPYFF VNYVDVSNAN VQTTVNSTML QQSFGRYWQK EVGLKAEILH
FQLSAFISKS QGSQLGKQQN VGVKLGYRW
