ID   HAGA1_PORGI             Reviewed;        2164 AA.
AC   P59915;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Hemagglutinin A;
DE   Flags: Precursor;
GN   Name=hagA; OrderedLocusNames=PG_1837;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
CC   -!- FUNCTION: Agglutinates erythrocytes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ66831.1; Type=Erroneous initiation; Evidence={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; AE015924; AAQ66831.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043876452.1; NC_002950.2.
DR   PDB; 3KM5; X-ray; 1.40 A; A/B=1137-1314.
DR   PDBsum; 3KM5; -.
DR   AlphaFoldDB; P59915; -.
DR   SMR; P59915; -.
DR   STRING; 242619.PG_1837; -.
DR   PRIDE; P59915; -.
DR   EnsemblBacteria; AAQ66831; AAQ66831; PG_1837.
DR   KEGG; pgi:PG_1837; -.
DR   PATRIC; fig|242619.8.peg.1698; -.
DR   eggNOG; COG1974; Bacteria.
DR   HOGENOM; CLU_232326_0_0_10; -.
DR   OMA; AFRHFGC; -.
DR   OrthoDB; 1063831at2; -.
DR   BioCyc; PGIN242619:G1G02-1715-MON; -.
DR   EvolutionaryTrace; P59915; -.
DR   Proteomes; UP000000588; Chromosome.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 4.
DR   InterPro; IPR011628; Cleaved_adhesin.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR018832; Pept_C25_gingipain_C.
DR   Pfam; PF07675; Cleaved_Adhesin; 8.
DR   Pfam; PF10365; DUF2436; 1.
DR   SMART; SM00060; FN3; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Hemagglutinin; Hydrolase; Protease; Reference proteome;
KW   Repeat; Signal; Thiol protease; Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..2164
FT                   /note="Hemagglutinin A"
FT                   /id="PRO_0000026537"
FT   REGION          26..539
FT                   /note="Peptidase C25-like 1"
FT   REGION          493..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..991
FT                   /note="Peptidase C25-like 2"
FT   REGION          992..1443
FT                   /note="Peptidase C25-like 3"
FT   COMPBIAS        494..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          1139..1141
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1156..1159
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1168..1171
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   TURN            1172..1174
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1181..1196
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1200..1204
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1213..1220
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1229..1236
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   HELIX           1240..1242
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1243..1249
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1263..1265
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1277..1282
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1289..1296
FT                   /evidence="ECO:0007829|PDB:3KM5"
FT   STRAND          1302..1311
FT                   /evidence="ECO:0007829|PDB:3KM5"
SQ   SEQUENCE   2164 AA;  233389 MW;  6DFAB22832586C63 CRC64;
     MRKLNSLFSL AVLLSLLCWG QTAAAQGGPK TAPSVTHQAV QKGIRTSKAK DLRDPIPAGM
     ARIILEAHDV WEDGTGYQML WDADHNQYGA SIPEESFWFA NGTIPAGLYD PFEYKVPVNA
     DASFSPTNFV LDGTASADIP AGTYDYVIIN PNPGIIYIVG EGVSKGNDYV VEAGKTYHFT
     VQRQGPGDAA SVVVTGEGGN EFAPVQNLQW SVSGQTVTLT WQAPASDKRT YVLNESFDTQ
     TLPNGWTMID ADGDGHNWLS TINVYNTATH TGDGAMFSKS WTASSGAKID LSPDNYLVTP
     KFTVPENGKL SYWVSSQEPW TNEHYGVFLS TTGNEAANFT IKLLEETLGS GKPAPMNLVK
     SEGVKAPAPY QERTIDLSAY AGQQVYLAFR HFGCTGIFRL YLDDVAVSGE GSSNDYTYTV
     YRDNVVIAQN LTATTFNQEN VAPGQYNYCV EVKYTAGVSP KVCKDVTVEG SNEFAPVQNL
     TGSAVGQKVT LKWDAPNGTP NPNPGTTTLS ESFENGIPAS WKTIDADGDG NNWTTTPPPG
     GSSFAGHNSA ICVSSASYIN FEGPQNPDNY LVTPELSLPN GGTLTFWVCA QDANYASEHY
     AVYASSTGND ASNFANALLE EVLTAKTVVT APEAIRGTRV QGTWYQKTVQ LPAGTKYVAF
     RHFGCTDFFW INLDDVEIKA NGKRADFTET FESSTHGEAP AEWTTIDADG DGQGWLCLSS
     GQLGWLTAHG GTNVVASFSW NGMALNPDNY LISKDVTGAT KVKYYYAVND GFPGDHYAVM
     ISKTGTNAGD FTVVFEETPN GINKGGARFG LSTEANGAKP QSVWIERTVD LPAGTKYVAF
     RHYNCSDLNY ILLDDIQFTM GGSPTPTDYT YTVYRDGTKI KEGLTETTFE EDGVATGNHE
     YCVEVKYTAG VSPKECVNVT VDPVQFNPVQ NLTGSAVGQK VTLKWDAPNG TPNPNPGTTT
     LSESFENGIP ASWKTIDADG DGNNWTTTPP PGGTSFAGHN SAICVSSASY INFEGPQNPD
     NYLVTPELSL PNGGTLTFWV CAQDANYASE HYAVYASSTG NDASNFANAL LEEVLTAKTV
     VTAPEAIRGT RVQGTWYQKT VQLPAGTKYV AFRHFGCTDF FWINLDDVEI KANGKRADFT
     ETFESSTHGE APAEWTTIDA DGDGQGWLCL SSGQLDWLTA HGGTNVVASF SWNGMALNPD
     NYLISKDVTG ATKVKYYYAV NDGFPGDHYA VMISKTGTNA GDFTVVFEET PNGINKGGAR
     FGLSTEANGA KPQSVWIERT VDLPAGTKYV AFRHYNCSDL NYILLDDIQF TMGGSPTPTD
     YTYTVYRDGT KIKEGLTETT FEEDGVATGN HEYCVEVKYT AGVSPKECVN VTVDPVQFNP
     VQNLTGSAVG QKVTLKWDAP NGTPNPNPGT TTLSESFENG IPASWKTIDA DGDGNNWTTT
     PPPGGTSFAG HNSAICVSSA SYINFEGPQN PDNYLVTPEL SLPNGGTLTF WVCAQDANYA
     SEHYAVYASS TGNDASNFAN ALLEEVLTAK TVVTAPEAIR GTRVQGTWYQ KTVQLPAGTK
     YVAFRHFGCT DFFWINLDDV EIKANGKRAD FTETFESSTH GEAPAEWTTI DADGDGQGWL
     CLSSGQLGWL TAHGGTNVVA SFSWNGMALN PDNYLISKDV TGATKVKYYY AVNDGFPGDH
     YAVMISKTGT NAGDFTVVFE ETPNGINKGG ARFGLSTEAN GAKPQSVWIE RTVDLPAGTK
     YVAFRHYNCS DLNYILLDDI QFTMGGSPTP TDYTYTVYRD GTKIKEGLTE TTFEEDGVAT
     GNHEYCVEVK YTAGVSPKEC VNVTINPTQF NPVQNLTAEQ APNSMDAILK WNAPASKRAE
     VLNEDFENGI PASWKTIDAD GDGNNWTTTP PPGGSSFAGH NSAICVSSAS YINFEGPQNP
     DNYLVTPELS LPGGGTLTFW VCAQDANYAS EHYAVYASST GNDASNFANA LLEEVLTAKT
     VVTAPEAIRG TRVQGTWYQK TVQLPAGTKY VAFRHFGCTD FFWINLDDVV ITSGNAPSYT
     YTIYRNNTQI ASGVTETTYR DPDLATGFYT YGVKVVYPNG ESAIETATLN ITSLADVTAQ
     KPYTLTVVGK TITVTCQGEA MIYDMNGRRL AAGRNTVVYT AQGGHYAVMV VVDGKSYVEK
     LAVK