ID A0A263HBV5_9PAST Unreviewed; 2271 AA.
AC A0A263HBV5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=RTX toxin protein {ECO:0000313|EMBL:SUU38477.1};
GN Name=cya_2 {ECO:0000313|EMBL:SUU38477.1};
GN ORFNames=NCTC10851_02112 {ECO:0000313|EMBL:SUU38477.1};
OS Actinobacillus seminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=722 {ECO:0000313|EMBL:SUU38477.1, ECO:0000313|Proteomes:UP000254507};
RN [1] {ECO:0000313|EMBL:SUU38477.1, ECO:0000313|Proteomes:UP000254507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10851 {ECO:0000313|EMBL:SUU38477.1,
RC ECO:0000313|Proteomes:UP000254507};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; UFSB01000001; SUU38477.1; -; Genomic_DNA.
DR InParanoid; A0A263HBV5; -.
DR OrthoDB; 1676884at2; -.
DR Proteomes; UP000254507; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 8.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR041690; Cadherin_5.
DR InterPro; IPR046742; DUF6792.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR010566; Haemolys_ca-bd.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF17892; Cadherin_5; 1.
DR Pfam; PF20591; DUF6792; 1.
DR Pfam; PF06594; HCBP_related; 1.
DR Pfam; PF00353; HemolysinCabind; 9.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51120; beta-Roll; 4.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 2271 AA; 246029 MW; B4EB1DBF690F0526 CRC64;
MSNDNLALLA AAAYGKFTDI KYDKEIQDAL KREHILTEPQ ATQFTATYEI LAHQANTANG
YSGTIVRNKH SHQVFVLHRG TEDVQDWVED GLLVLGGLPY RQIVDAKKFV DENIKNGNIS
GDFTNVGHSL GKSIADIVHF TTDLSSGSIG FNGAGSSFLG DGQKVNISIP AWDISNLVKQ
SGNRKLLEKL AKESGNVFDP SKSNVKNFVS LGPSIVASHL PYHQHGKIIS FNNGTTASHS
ISPFIEPMDW VVKLSDKYQI GLEEAVNLYN INGQYAYSFD KKYGKPGYDL DKAHEVLNRY
MSENKNISAT NLELYAKNEY LSHRGGISSM IDIGKNRYWP NYGLKSDNKV YIGNTDAIPS
DYDSFYVTNQ NKISFNKDVL NKSTKTSDLA SSSILTDDRR IANHNLIAMK AIEVANMAVS
AIPKVRTPKI NTLLNSSQGK PYKIAIDPLI LDLNGDGAKA VSYSDKSVLF DIDNDGGSLE
ETGWLSNQDG LLVQDLNNNG KIDNMAEVFS EYYAGKAGRN GESGEKRFKN GFEALSTLDS
NRDRVFDHKD KGFNSVRVWQ DKNHNGITDK GELQTLADLG ITSVDLRYQD AGGQLFYGNE
LLAKGNFTRK GKKYEAAAVN FLANPRGHII TSMAGGKKTV TEAAGVLAKT GSFTAADDVA
RTLEAKRLGV ENIQAGNGND TLYGDERDNW LAGGGGKDTF YGGDGDDVLL IDGEDLPENI
HGGKGNDVVQ VIGNQGVSLD LGKAEIEIAH GGRGNDVFFS SGNSSVFVRG GDGNDTIIGS
IANDALSGEN GNDSLSGNAG NDLIRGHRGN DRLFGDDGDD ILFGGSDDDI LHGGYGNDTL
LGEGGDDYLD GGEGEDTAEF SGNFADYKIT KMGEGILISD KTQGRDGTDF LRNIERLNFK
DITNYLAPTA DNEWENPIPV EDILYQDSKG QRFDGTRPYI IKPSQLLKND IDLQGDNLVI
YQASNIRGGS LKELANGDIE FTPLKGFNGI AGFEYSIKDS KDVTSVGTQG KGELTGKVYL
VPPHLPSDPD VIRQHYLDAA NILPVWAQYS GKNIRIGQFE PSGPFSIAEE VADYRHFELR
NKVDKSWLHD YEYKRQEDDK VFSKHATEVA GIMVAERNGE GGVGVAYDAT VASYWVGADV
SGLDKMKYYD VANHSWGHTQ NFRQQISFSD KSKTIFDLYK PALTEGRHGL GTVIVNSAGN
DRAKGGNTNY SELTNVRYGI AVASAELNAA FETKIAGYSN PGASVLVTAH GSNAYSCSRE
IVNENGSVLG EEYARNNGTS YSAPVVSGIV ALMLEANPYL GYRDIQEILA LTATTKGITD
SQWQRNGAKN WNGTGMHVSH DYGYGIVDAQ AAVRLAQNWN TQHTYDNEVK LESVFQSEPL
KLAIDDNSGI QSSVEVSNAK IQLENVSVKL NLTHPRAGDL IVKLISPAGT ESILMNRAGK
DPNDESATGE VKFGESSTLN YTFNTALLKG EDPNGKWALQ VFDVATGETG TLNHWSLSFY
GRTYDGSDTY VYTNEFHNNQ ISHQLNDTNG GVDTINASAM DGVINVDLLS GKADLAGKAL
TVQNPQHIEN IIGGDFNDVL SGNNGVNVLV GGRGNDILSG LAGNDVLVGG LGKNTLTGGE
GSDTFIIEKK SSGEDVIVDF KVGTDRLVLT GFDPLNVPTK AQQGKDTVIT LQEQIIRLKN
IKADSFLMDN IVLTKEVFKP YWLNQRDAYG FANSNDEVAL PHMGVAFWGT ERDDRLFGGN
GNDIIRGGSG RDIIVGEHAA DSVMGGNDIL YGDGGDDRIM GGGGNDTLYG GMGDDYLGGG
AGDDIIYLEG DDTALSNSYR NQQYITLGQY NDVEFSWARG EGGSGSDRFV IVKDNSGNAS
KGLLKNLIWD FDLNDKNEKI DLSQFKGLHT VNISGFAVNG EQYSRIWLGE AKAGTQYITL
RGISPDKIKE EMFIFSNEQA DLPQLTYSIS GSNKNDTLKG NAIGNVIDGK AGSDVMEGFA
GDDVYSVDNV GDKVIEAKNE GYDTVKSSVS YTLPNHVEEL QLTKNASING TGNAENNRLV
GNSGNNRLDG KAGFDTMIGK AGNDTYIVDS HLDKVIEKPG EGHDTVISSV SYTLPENVEH
LALSGNHPIS GTGNDKNNTI KGNAADNRLI GYEGNDTLNG MRGNDFLMGG KGNDTYQFNR
GDGIDTIYDE QGEDTLRFTN VNHNQLWFRK LDTDLEVSVI GTQDKVIIAD WYAKNYKIET
IVAANNKSLA HSDVDKLISA MSAFAPPTAG QISLPQEINA KINPVLAANW I
//
