ID W1ITI6_9GAMM Unreviewed; 1027 AA.
AC W1ITI6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 02-APR-2025, entry version 43.
DE SubName: Full=Putative Extracellular serine protease {ECO:0000313|EMBL:CDL80530.1};
GN ORFNames=XSR1_10016 {ECO:0000313|EMBL:CDL80530.1};
OS Xenorhabdus szentirmaii DSM 16338.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL80530.1, ECO:0000313|Proteomes:UP000019202};
RN [1] {ECO:0000313|EMBL:CDL80530.1, ECO:0000313|Proteomes:UP000019202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL80530.1,
RC ECO:0000313|Proteomes:UP000019202};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT 16338.";
RL Submitted (NOV-2013) 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:CDL80530.1}.
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DR EMBL; CBXF010000001; CDL80530.1; -; Genomic_DNA.
DR RefSeq; WP_038233476.1; NZ_CAWLWS010000001.1.
DR AlphaFoldDB; W1ITI6; -.
DR STRING; 1427518.XSR1_10016; -.
DR GeneID; 97123676; -.
DR OrthoDB; 9780507at2; -.
DR Proteomes; UP000019202; Unassembled WGS sequence.
DR GO; GO:0019867; C:outer 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; 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; IPR006315; OM_autotransptr_brl_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR051048; Peptidase_S8/S53_subtilisin.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034061; Peptidases_S8_Autotransporter.
DR NCBIfam; TIGR01414; autotrans_barl; 1.
DR NCBIfam; TIGR02601; autotrns_rpt; 1.
DR PANTHER; PTHR43399:SF4; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF12951; PATR; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; Autotransporter; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 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}; Reference proteome {ECO:0000313|Proteomes:UP000019202};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1027
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004803733"
FT DOMAIN 750..1027
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
FT ACT_SITE 79
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 117
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1027 AA; 111679 MW; 363C751386E008F8 CRC64;
MKKTNSVRPI FLWMTLFFGL LPVNSSIAST EYQEQGKNNS PESWLSEEFK NQWGLAAIGA
HYAYARGYTG KGINVGILDE AVSDHPEFAG KHKILSPEDI WNYDEDEDSG IITFGAHGNH
VSGTIAANRD GKGMHGVAFD AGLITGKYLQ NIYNRTEAMI QSDARIINNS WGVRPVVRRD
KDGWPIKLPN GTYDYVKVTL QDVINFVTPM KEELDELSRS PIPEFDDYIT RSAGLLRAAR
QGKLVVFAAG NANNYNVTWL HAGMPYFFPD ALKNYLSVAN LNQNGELNPS STSCGYTASY
CLSAPGTKIY SSTGDFVSKV DGDINEDALA NNELAIDPTY DTYTGTSMAS PHVAGAAAIL
MQRFPYMTTG QISDVLKTTA TDLGEKGLDN LYGWGMLNLK DAIDGPKMFI TEQDIPKEFY
IPGSYTDTQF IANIPGWGAE VESGTTVART CESIECVYDS WSNDIGGHGG LTKTGKGVLD
LAGKNSTYKG PTLVEQGVLQ VSGSITSDVT VQENAMFAGA GSVGSIMLNA GAAISPGNLI
EPGEVSTNGT LTVERDITFQ KGSHYRVEVA PDSPGYSDRI ISNGLATLKG GQVQVALESS
RNLLAKQEVR SLLGQQYNIL QANKGINGQF EAVVPNYLFM GAELNYQPDR VMLNLKRNSK
TFESFAKTAN ERAVARAADN LGLGHPVYES ILMLDTGEQV HQASMAFQQL STSQIHDDIA
TAQVNSSRYL RDTLNTRLRQ ADNGNIGQGI KSNQNGVWAQ ILGNWQRTSG NSDVNGYRVS
NYGVLLGADK DLGNDWRFGV TTGYTRSSLK GSHSTSARSD NFHLGLYGSK QIDALALRAG
TAYSWHRFDT ERSVAFSSQS DNLKAKYGAQ TAQLFTEAAY GIDTSLLNLE PFANLSYVNF
RNNKINEHGG AAALHGDKQS KNATFSTLGL RADKKWKAEN EMTVSLYGEL GWQHQFGSVD
RGTKLSFSNS NSAFTIKSVS PERDSAVIKV GTELGINEKA KLSLGYNGVV SSNNKDNGVF
LNANWTF
//
