ID E6KUU3_9ACTO Unreviewed; 2174 AA.
AC E6KUU3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Choline-binding protein {ECO:0000313|EMBL:EFU60246.1};
GN ORFNames=HMPREF9006_1995 {ECO:0000313|EMBL:EFU60246.1};
OS Actinomyces sp. oral taxon 180 str. F0310.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=888052 {ECO:0000313|EMBL:EFU60246.1, ECO:0000313|Proteomes:UP000006252};
RN [1] {ECO:0000313|EMBL:EFU60246.1, ECO:0000313|Proteomes:UP000006252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0310 {ECO:0000313|EMBL:EFU60246.1,
RC ECO:0000313|Proteomes:UP000006252};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFU60246.1}.
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DR EMBL; AEPP01000037; EFU60246.1; -; Genomic_DNA.
DR RefSeq; WP_009213434.1; NZ_GL622194.1.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR HOGENOM; CLU_231546_0_0_11; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000006252; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 2.
DR Gene3D; 2.20.120.10; Multimodular pneumococcal cell wall endolysin, domain 3; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR034216; C5a_Peptidase.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF19127; Choline_bind_3; 2.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF13306; LRR_5; 3.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00635; BID_2; 2.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51170; CW; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..2174
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003207477"
FT DOMAIN 1116..1193
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 1202..1286
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT REPEAT 2153..2172
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 31..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1965..1989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1970..1984
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 284
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 628
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 2174 AA; 227704 MW; A383E8BC0D8F3C7E CRC64;
MSHRKISALV LATVGALAMT TVSIPAAFAA DAREESQSGA PASSVDARSG APQSGSSDEA
GAENPTTTPE SFPSDDTPTT IIVQLEDGAV GIPWYRRIFG LSSSTKHETV KDRIETAVEA
AVPGADITDV RDYTHALDGF AIQAPASSLD AIKATEGVKA AFIERHHKPM VVEGDGGALG
VEAVDPALQN ASSLEMTRAN QTAQKGERQV VEVIDTGIEA THQAFSGSMD GVDVRMSQAD
VEAFAATLPH GKTGSYINKK IPFVFDYADN DPDVLPKSSK DLSHGTHVAA IAAANAADLQ
GTAPHAQIIV AKVASDKDGS IPDSTVLAAL DDAVVIKPDS INLSLGEDAG MGTEAGTVYA
DVYKNLAAAG VTVNAAAGNS YSSAYSNKSG KNRPYATDPD AGTLSEPASY SSTLAVASVN
NQDALPYLTV GDRKVVYRKS RGLKDAVVPS LRDIEEGTYT LVYAGIGDAA ALDKLVAEHP
GDLSKVIVLE DRGGSDSATG ADMTHEAKVK GLTQLASKPA ALIIGDSEVA ETPYVATIEA
THTMPTVTIT QKEKDTLIEA ITASESGSIT IANPHSGLQL ASTNPSISDF TSWGVTPDLK
LKPEIAAPGG NIVAAVLGNT YRSMSGTSMA TPQVAGIATL VRQRVNEDPA FAGLSDAEKT
AVVTNLMMGT AHPLLDIDQN NGTYYSPRRV GAGQVDALAA TTTFVYPSVV GAENPWRPKA
DLGEGTNGWT FQVTLTNVSD TARTYTLGGQ ALSEIVDGEL FTEHSKNWAG QGIDLTFSAG
SVTVPAKGTS TVSVTVTPQA AFASYANANA PKGTFIDGAV TFTSADGAPD LTVPYMGFYG
SWGSPAVFDA KWFDGTTNAV HSCASTLLNP ATEVPLGALN PLVGQEIDDV RAVDPAYFIM
SRSALPDAPS RLLPRTCLLR NSPKVTYTYT NEAGDVVREY TFERARKSLF NYHASRIEPI
ESQEGNNPVF DGFDKDGKEL PAGRYKLTID AASVAPSSVS SQMTWDFTLD TQAPVISNLV
VTGEGDARVV SFDVTDNSPL AGIAFSESPT SRHYYDEKEA VGANRQADGT YAKHYEIKWA
DLIDRADSSD PATAYLFAWD WGKNQARQVI RFRTIPMTSL SVTPESSSVV AGETVALSAS
YEPASANVTD LVWTSSNEAV ATVNDNGEVQ TLAAGDATIT ATDASQSTLS ASAQVHVRTI
SEDAGIEVAE AAVSVKVGES APVKAYLAPS LKDRAVTWSV EPADLATVVA DTDTDTRKAT
LTAGDHAGSG TLTATVTTEG GAVKTATIPV TVRAADADDF EINEEGVLVK YKGSATDVTI
PETVTSIAER AFASSSVENV TIPASVRSIG QEAFIYSSLK TIAFVDDAAR PAQLTTIADR
AFANTSLQAI ELPRSVVTIG AGVFDYNSAL TSIKLGPNVD ASSVTGGYAE TSALMSVEVD
PANPNFDSVD GVLYSKDHSK LIIYPAAKNA GGAYTVLDGV QAIAYRAFQK ASITSVTLPD
SLRSIGEEGF RLSALTAVAL PEKFETLGVC AFCSADKLDS IDLGGTITVG GSAFESTKAK
AGINFRPELG RLATIGDFAF SRTAPASVAL PDSVTTVGEQ AFSENTALTS FHIGSGVTSF
AETALYNDRK IATLTVAPAN AVYSAERNVL YRKADDGLHL MLSPAANTLT DYTVRAGTVE
IGASAFANNK SLTRVVLPEG VTTIGDDAFA GCTALTDLVI PDSMERSSGV VGNSLEVVEY
GTKIRSIRME GSWVPMPRRI VVRGGQDGSF VYDGRPTNGR RQSAFFGEGM TSVSFGVDVP
RILVLPSTLT RLDLEAELSE EKKDDTHVYV AATEGEPAWN VAKAALDAAG IDASHLHAYV
LASVSLSGTN IAEAGGSYTY TGEVGASVDV TATAAGGIAG THEVRAVQVG ADGAETLVRD
WTTLTGGEDR AATASATFPW TPSSADVRLR VQVRDASYLT NTAVVNLPGA PTPDPDPAPN
PDPAPKDGKW VSDSRGWWYR YSDGSYPVSE RVAIGGQVYR FGADGYMRTG WVSEQGSWFF
HGGSGAEASG WVKDGGSWYY LAPGSGAMAT GWVKDGDSWY YLTPGSGAMA TGWVKDGDSW
YYLTPGSGAM ATGWVKDGGT WYYLAPGSGA MATGWVQDRG SWYYLTPGSG AMATGWIRID
GQWYHFTASG RWVG
//
