PGBB_HELPJ
ID PGBB_HELPJ Reviewed; 541 AA.
AC Q9ZKY5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Plasminogen-binding protein PgbB;
GN Name=pgbB; OrderedLocusNames=jhp_0797;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: Binds plasminogen, specifically, and in a concentration and
CC lysine-dependent manner. Plasminogen is the precursor of plasmin, a
CC serine protease that cleaves fibrin, fibronectin, laminin and
CC vitronectin. Acquisition of plasminogen/plasmin could enable H.pylori
CC to degrade host components (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000305}. Note=The plasminogen-
CC binding region is localized on the surface the bacterium.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Plasminogen bound to PgbB is capable of being converted
CC to functionally active plasmin. {ECO:0000250}.
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DR EMBL; AE001439; AAD06373.1; -; Genomic_DNA.
DR PIR; H71887; H71887.
DR RefSeq; WP_001039534.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZKY5; -.
DR SMR; Q9ZKY5; -.
DR STRING; 85963.jhp_0797; -.
DR PRIDE; Q9ZKY5; -.
DR EnsemblBacteria; AAD06373; AAD06373; jhp_0797.
DR KEGG; hpj:jhp_0797; -.
DR PATRIC; fig|85963.30.peg.175; -.
DR eggNOG; ENOG50316V3; Bacteria.
DR OMA; NESQGFF; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR032737; PGBA_C.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF15437; PGBA_C; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
FT CHAIN 1..541
FT /note="Plasminogen-binding protein PgbB"
FT /id="PRO_0000058352"
FT REGION 420..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 61715 MW; 3232E0A398B69B1E CRC64;
MNKPFLILLI ALIAFSGCNM RKYFKPAKHQ IKGEAYFPNH LQESIVSSNR YGAILKNGAV
IGDKGLTQLR IGKNFNYESS FLNESQGFFI LAQDCLNKID KKTSKSRAAK TEETELKLKG
VEAEVQDKVC HQVELISNNP NASQQSIVIP LETFALSASV KGNLLAVVLA DNSANLYDIT
SQKLLFSEKG SPSTTINSLM AMPIFMDTVV VFPMLDGRLL VVDYVHGNPT PIRNIVISSD
KFFNNITYLI VDGNNMIAST GKRILSVVSG QEFNYDGDIV DLLYDKGTLY VLTLDGQILQ
MDKSLRELNS VKLPFASLNT IVLNNNKLYS LEKRGYVIEV DLNDFDSYNV YKTPTIGSFK
FFSSNRLDKG VFYDKNRVYY DRYYLDYNDF KPKLYPHAAE FKTSQKGEKG NAPIYLQERH
KAKENKQPLE ENKVKPRNSG FEEEEVKTRR PEPTKDQNNA IQQGETKNNE SKNTPISKEN
AAKKEAPKPS SKEEKRRLKE EKKKAKAEQR AREFEQRARE HQERDEKELE ERRKALEMNK
K