ID   HAGA2_PORGN             Reviewed;        2628 AA.
AC   Q51845;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Hemagglutinin A;
DE   Flags: Precursor;
GN   Name=hagA;
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-1703 / FDC 381;
RX   PubMed=8926061; DOI=10.1128/iai.64.10.4000-4007.1996;
RA   Han N., Whitlock J., Progulske-Fox A.;
RT   "The hemagglutinin gene A (hagA) of Porphyromonas gingivalis 381 contains
RT   four large, contiguous, direct repeats.";
RL   Infect. Immun. 64:4000-4007(1996).
CC   -!- FUNCTION: Agglutinates erythrocytes.
CC   -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000305}.
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DR   EMBL; U41807; AAB17128.1; -; Genomic_DNA.
DR   PIR; T28651; T28651.
DR   AlphaFoldDB; Q51845; -.
DR   SMR; Q51845; -.
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; -; 5.
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; 10.
DR   Pfam; PF10365; DUF2436; 1.
DR   SMART; SM00060; FN3; 6.
PE   3: Inferred from homology;
KW   Hemagglutinin; Hydrolase; Protease; Repeat; Signal; Thiol protease;
KW   Virulence.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..2628
FT                   /note="Hemagglutinin A"
FT                   /id="PRO_0000026538"
FT   REGION          25..539
FT                   /note="Peptidase C25-like 1"
FT   REGION          493..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..995
FT                   /note="Peptidase C25-like 2"
FT   REGION          944..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          996..1451
FT                   /note="Peptidase C25-like 3"
FT   REGION          1400..1458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1452..1907
FT                   /note="Peptidase C25-like 4"
FT   REGION          1856..1881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1890..1909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2074..2628
FT                   /note="Peptidase C25-like 5"
FT   REGION          2336..2358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        983..1002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1439..1458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1895..1909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2342..2358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2628 AA;  283325 MW;  61C4DE32540C99DA CRC64;
     MRKLNSLFSL AVLLSLLCWG QTAAAQGGPK TAPSVTHQAV QKGIRTSKVK DLRDPIPAGM
     ARIILEAHDV WEDGTGYQML WDADHNQYGA SIPEESFWFA NGTIPAGLYD PFEYKVPVNA
     DASFSPTNFV LDGTASADIP AGTYDYVIIN PNPGIIYIVG EGVSKGNDYV VEAGKTYHFT
     VQRQGPGDAA SVVVTGEGGN EFAPVQNLQW SVSGQTVTLT WQAPASDKRT YVLNESFDTQ
     TLPNGWTMID ADGDGHNWLS TINVYNTATH TGDGAMFSKS WTASGGAKID LSPDNYLVTP
     KVTVPENGKL SYWVSSQVPW TNEHYGVFLS TTGNEAANFT IKLLEETLGS DKPAPMNLVK
     SEGVKLPAPY QERTIDLSAY AGQQVYLAFR HFNSTGIFRL YLDDVAVSGE GSSNDYTYTV
     YRDNVVIAQN LAATTFNQEN VAPGQYNYCV EVKYTAGVSP KVCKDVTVEG SNEFAHVQNL
     TGSAVGQKVT LKWDAPNGTP NPNPGTTTLS ESFENGIPAS WKTIDADGDG NNWTTTPPPG
     GTSFAGHNSA ICASSASYIN FEGPQNPDNY LVTPELSLPN GGTLTFWVCA QDANYASEHY
     AVYASSTGND ASNFANALLE EVLTAKTVVT APEAIRGTRV QGTWYQKTVQ LPAGTKYVAF
     RHFGCTDFFW INLDDVEIKA NGKRADFTET FESSTHGEAP AEWTTIDADG DGQGWLCLSS
     GQLDWLTAHG GTNVVASFSW NGMALNPDNY LISKDVTGAT KVKYYYAVND GFPGDHYAVM
     ISKTGTNAGD FTVVFEETPN GINKGGARFG LSTEADGAKP QSVWIERTVD LPAGTKYVAF
     RHYNCSDLNY ILLDDIQFTM GGSPTPTDYT YTVYRDGTKI KEGLTETTFE EDGVATGNHE
     YCVEVKYTAG VSPKECVNVT VDPVQFNPVQ NLTGSAVGQK VTLKWDAPNG TPNPNPNPNP
     GTTTLSESFE NGIPASWKTI DADGDGNNWT TTPPPGGTSF AGHNSAICAS SASYINFEGP
     QNPDNYLVTP ELSLPNGGTL TFWVCAQDAN YASEHYAVYA SSTGNDASNF ANALLEEVLT
     AKTVVTAPEA IRGTRVQGTW YQKTVQLPAG TKYVAFRHFG CTDFFWINLD DVEIKANGKR
     ADFTETFESS THGEAPAEWT TIDADGDGQG WLCLSSGQLG WLTAHGGTNV VASFSWNGMA
     LNPDNYLISK DVTGATKVKY YYAVNDGFPG DHYAVMISKT GTNAGDFTVV FEETPNGINK
     GGARFGLSTE ADGAKPQSVW IERTVDLPAG TKYVAFRHYN CSDLNYILLD DIQFTMGGSP
     TPTDYTYTVY RDGTKIKEGL TETTFEEDGV ATGNHEYCVE VKYTAGVSPK ECVNVTVDPV
     QFNPVQNLTG SAVGQKVTLK WDAPNGTPNP NPNPNPGTTT LSESFENGIP ASWKTIDADG
     DGNNWTTTPP PGGTSFAGHN SAICASSASY INFEGPQNPD NYLVTPELSL PNGGTLTFWV
     CAQDANYASE HYAVYASSTG NDASNFANAL LEEVLTAKTV VTAPEAIRGT RVQGTWYQKT
     VQLPAGTKYV AFRHFGCTDF FWINLDDVEI KANGKRADFT ETFESSTHGE APAEWTTIDA
     DGDGQGWLCL SSGQLGWLTA HGGTNVVASF SWNGMALNPD NYLISKDVTG ATKVKYYYAV
     NDGFPGDHYA VMISKTGTNA GDFTVVFEET PNGINKGGAR FGLSTEADGA KPQSVWIERT
     VDLPAGTKYV AFRHYNCSDL NYILLDDIQF TMGGSPTPTD YTYTVYRDGT KIKEGLTETT
     FEEDGVATGN HEYCVEVKYT AGVSPKECVN VTVDPVQFNP VQNLTGSAVG QKVTLKWDAP
     NGTPNPNPNP NPGTTTLSES FENGIPASWK TIDADGDGNN WTTTPPPGGT SFAGHNSAIC
     VSSASYINFE GPQNPDNYLV TPELSLPGGG TLTFWVCAQD ANYASEHYAV YASSTGNDAS
     NFANALLEEV LTAKTVVTAP EAIRGTRVQG TWYQKTVQLP AGTKYVAFRH FGCTDFFWIN
     LDEVEIKANG KRADFTETFE SSTHGEAPAE WTTIDADGDG QGWLCLSSGQ LDWLTAHGGT
     NVVASFSWNG MALNPDNYLI SKDVTGATKV KYYYAVNDGF PGDHYAVMIS KTGTNAGDFT
     VVFEETPNGI NKGGARFGLS TEADGAKPQS VWIERTVDLP AGTKYVAFRH YNCSDLNYIL
     LDDIQFTMGG SPTPTDYTYT VYRDGTKIKE GLTETTFEED GVATGNHEYC VEVKYTAGVS
     PKVCVNVTIN PTQFNPVQNL TAEQAPNSMD AILKWNAPAS KRAEVLNEDF ENGIPSSWKT
     IDADGDGNNW TTTPPPGGSS FAGHNSAICV SSASYINFEG PQNPDNYLVT PELSLPGGGT
     LTFWVCAQDA NYASEHYAVY ASSTGNDASN FANALLEEVL TAKTVVTAPE AIRGTRVQGT
     WYQKTVQLPA GTKYVAFRHF GCTDFFWINL DDVVITSGNA PSYTYTIYRN NTQIASGVTE
     TTYRDPDLAT GFYTYGVKVV YPNGESAIET ATLNITSLAD VTAQKPYTLT VVGKTITVTC
     QGEAMIYDMN GRRLAAGRNT VVYTAQGGHY AVMVVVDGKS YVEKLAVK