ID A1KSW3_NEIMF Unreviewed; 1568 AA.
AC A1KSW3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=IgA-specific serine endopeptidase {ECO:0000256|ARBA:ARBA00038992};
DE EC=3.4.21.72 {ECO:0000256|ARBA:ARBA00038992};
GN Name=iga {ECO:0000313|EMBL:CAM09944.1};
GN OrderedLocusNames=NMC0651 {ECO:0000313|EMBL:CAM09944.1};
OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS 15464 / FAM18).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=272831 {ECO:0000313|EMBL:CAM09944.1, ECO:0000313|Proteomes:UP000002286};
RN [1] {ECO:0000313|EMBL:CAM09944.1, ECO:0000313|Proteomes:UP000002286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700532 / DSM 15464 / FAM18
RC {ECO:0000313|Proteomes:UP000002286};
RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA Quail M.A., Achtman M., Barrell B., Saunders N.J., Parkhill J.;
RT "Meningococcal genetic variation mechanisms viewed through comparative
RT analysis of serogroup C strain FAM18.";
RL PLoS Genet. 3:230-240(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of immunoglobulin A molecules at certain Pro-|-Xaa
CC bonds in the hinge region. No small molecule substrates are known.;
CC EC=3.4.21.72; Evidence={ECO:0000256|ARBA:ARBA00035943};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|ARBA:ARBA00004571}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004571}. Cell surface
CC {ECO:0000256|ARBA:ARBA00004241}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Periplasm
CC {ECO:0000256|ARBA:ARBA00004418}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; AM421808; CAM09944.1; -; Genomic_DNA.
DR RefSeq; WP_002221261.1; NC_008767.1.
DR SMR; A1KSW3; -.
DR MEROPS; S06.001; -.
DR KEGG; nmc:NMC0651; -.
DR HOGENOM; CLU_004023_0_0_4; -.
DR Proteomes; UP000002286; 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:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR CDD; cd01343; PL1_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 3.30.160.280; -; 1.
DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR InterPro; IPR004899; Pertactin_central.
DR PANTHER; PTHR12338:SF9; ANTIGEN 43; 1.
DR PANTHER; PTHR12338; AUTOTRANSPORTER; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02395; Peptidase_S6; 1.
DR Pfam; PF03212; Pertactin; 1.
DR PRINTS; PR00921; IGASERPTASE.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; Autotransporter; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAM09944.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CAM09944.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1568
FT /note="IgA-specific serine endopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002635805"
FT DOMAIN 28..311
FT /note="Peptidase S6"
FT /evidence="ECO:0000259|PROSITE:PS51691"
FT DOMAIN 1316..1568
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
FT REGION 969..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1568 AA; 172738 MW; 45318F9F9E066FFF CRC64;
MKTKRFKINA ISLSIFLAYA LTPYSEAALV RDDVDYQIFR DFAENKGKFF VGATDLSVKN
KQGQNIGNAL SNVPMIDFSV ADVNRRTLTV IDPQYAVSVK HVKGDEISYY GHHNGHLDVS
NDENEYRSVA QNDYEPNKNW HHGNQGRLED YNMARLNKFV TEVAPIAPTS AGGGVETYKD
KNRFSEFVRV GAGTQFEYNS RYNMTELSRA YRYAIAGTPY QDVNVTSNLN QEGLIGFGDN
SKHHSPEKLK EVLSQNALTN YAVLGDSGSP LFAYDKQEKR WVFLGAYDYW AGYQKNSWQE
WNIYKKEFAD KIKQRDNAGT IKGNGEHHWN ITFGTNSKIG STAVRLAGNE KDANNGQNVT
FEDNGTLVLD QNINQGAGGL FFKGDYTVKG INNDITWLGA GIDVTDGKKV VWQVKNPNGD
RLAKIGKGTL EINGTGVNQG QLKVGDGTVI LNQQADADKK VQAFSQVGIV SGRGTLVLNS
SNQINPDNLY FGFRGGRLDA NGNDLTFEHI RNVDEGARIV NHNTSHASTI TLTGKSLITN
PNSLSVHSIQ NDYDEDDYSY YYRPRRPIPQ GKDLYYKNYR YYALKSGGSV NAPMPENGVT
ENNDWVFMGY TQEEAKKNAM NHKNNQRISG FSGFFGEENG KGHNGALNLN FNGKSAQNRF
LLTGGTNLNG KISVTQGNVL LSGRPTPHAR DFVNKSSARK DAHFSKNNEV VFEDDWINRT
FKAAEIAVNQ SASFSSGRNV SNITANITAT DNAKVNLGYK NGDEVCVRSD YTGYVTCNTG
NLSDKALNSF GATQINGNVN LNQNAALVLG KAALWGQIQG QGNSRVSLNQ HSKWHLTGDS
QVHNLSLADS HIHLNNASDA QSANQYHTLK INHLSGNGHF HYLTHLAENL GDKVLVKESA
SGHYQLHVQD KTGEPNQEGL NLFDASSVQD RSRLSVSLAN NHVDLGALRY TIKTENGITR
LYNPYAENRR RVKPVPSPAT NTASQAQTDS AQIAKPQNIV VAPPSPQANQ AEEAKRQQAK
AEQVKRQQAE AERKSAELAK QKAEAEREAR ELATRQKAEQ ERSSAELARR HEKEREAAEL
SAKQKVEAER EAQALAVRRK AEAEEAKRQA AELARQQEEA RKAAELAAKQ KAETERKAAE
IAEQKAEAER EAAELAKQKA EEEGRQAAQS QPKRRNRRAI PPELSSDATT RALPRIARNS
NPDASDYEEI PLDALEDEDV SESVDTSDKQ PQDNTELHEK VETVSLQPRA AQPRAQAAAQ
PQAQAAAQPQ AQAVAQADAV STNTNSALSD AMASTQSILL DTGASLTRHI AQKSRADAEK
NSVWMSNIGY GRDYASAQYR RFSSKRTQTQ IGIDRSLSEN MQIGGVLTYS DSQHTFDQAS
GKNTFVQANL YGKYYLNDAW YVAGDIGAGS LRSRLQTQQK ANFNRTSIQT GLTLGNTLKI
NQFEIVPSAG IRYSRLSSAD YKLGNDSVKV SSMSVKTLTA GLDFAYRFKV GNLTVKPLLS
AAYFANYGKG GVNVGGNSFA YKADNQQKYS AGAALLYRNV TLNVNGSITK GKQLEKQKSG
QIKIQIRF
//
