ID C9N1N9_9FUSO Unreviewed; 999 AA.
AC C9N1N9;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Outer membrane autotransporter barrel domain protein {ECO:0000313|EMBL:EEX73432.1};
GN ORFNames=GCWU000323_02761 {ECO:0000313|EMBL:EEX73432.1};
OS Leptotrichia hofstadii F0254.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=634994 {ECO:0000313|EMBL:EEX73432.1, ECO:0000313|Proteomes:UP000006233};
RN [1] {ECO:0000313|EMBL:EEX73432.1, ECO:0000313|Proteomes:UP000006233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0254 {ECO:0000313|EMBL:EEX73432.1,
RC ECO:0000313|Proteomes:UP000006233};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC 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:EEX73432.1}.
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DR EMBL; ACVB02000029; EEX73432.1; -; Genomic_DNA.
DR RefSeq; WP_006806047.1; NZ_GG700634.1.
DR AlphaFoldDB; C9N1N9; -.
DR STRING; 634994.GCWU000323_02761; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4625; Bacteria.
DR HOGENOM; CLU_005887_0_0_0; -.
DR Proteomes; UP000006233; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04848; Peptidases_S8_Autotransporter_serine_protease_like; 1.
DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR013425; Autotrns_rpt.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR034061; Peptidases_S8_Autotransporter.
DR NCBIfam; TIGR02601; autotrns_rpt; 1.
DR PANTHER; PTHR35037; C-TERMINAL REGION OF AIDA-LIKE PROTEIN; 1.
DR PANTHER; PTHR35037:SF3; C-TERMINAL REGION OF AIDA-LIKE PROTEIN; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF12951; PATR; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; Autotransporter; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Reference proteome {ECO:0000313|Proteomes:UP000006233};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..999
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002998154"
FT DOMAIN 713..999
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
FT REGION 18..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 999 AA; 106771 MW; 55760CDB7FF52912 CRC64;
MKKILLLASL ITALSSCGGG GGGGGSSQTG SATPVPTPSQ PGGNTNNQAQ NPNLPNNNGQ
TQNNPSQSES NNNNSSTSQV PKNSDFTGRG VSVAVLDSDF LSSDVHTNQL YNKRSYIDEI
IDREFKDRFI KEPIVTNAAY LSKSNHGILV ASILGGNSGT GATGAKIHGV SVSQGSGFYL
DIDKYQDLQN KGVRIYSHSF GTQQTLGEFN FNNFREPFRI YLRKLGETIA LSENDNRVNN
LINFYRNAVD QGSLFIWAAG NRRADGTTMD EASIQAGLPY YVSGLYKGWI AVMGVRPDGT
EYNPHLARAR RAMWWTVAAN GECGLPGCTE YGSSFATPKV SAAAAKLKEK FPWMTGHEIQ
QTILTTATDL GQPGVDEIFG WGLLNEEKAL KGPAKFSREL LVGERAANAG LSGQFNANVG
DNITSTFENN ITGLGGLKKS GNGTLILAGN NTYQGSTDIE SGTLIVEKEN GSPITIKSGG
TLVTTPTTII GLKTYSGNLS PVNVKNEGGT LENRGSGAVI TGDYTATAGS VTKAEIGTKL
IVRGAVNLNG GNTTLQALSN GKYITAKTMS SAVIEAEKGI NGNFDKVETP ELINGAVETS
DNKINVKLSR KNVLEYAEKI AESDEMQKNT AQNLETAFQN LDENIENGTA GNVAQFERKA
AKLQSLNHSN RAAVLDSLSG QIYASAQALT FQHSQTVNKD LSNRLVMLGT LDNPGDNFGL
WISGLGANGT LKQDGYGKGD TKVSGGQVGV DRQFGENLIL GTALSYSKAN VKFNRYGGKS
DANNFGVSLY GRLGNKNVPF YLQGRLGIGF VDSDVERDII LSSNDYTRAK INHNDKVYSG
YLETGYDIRN SNGDFVVTPF AGLTHDTVVR GSFSEEKSQF GLTADKKNYN QTSALLGVRV
GKAVNWNGGS KTTFQGYVTH QRAFNDQDLS FDARYTGLPG ATFKVKGIGL AKNKTWAGVG
ALTEVNSKFG WYVNYDGSVD SGKGKGNNNV FTTGLRFNF
//
