ID D1ALR9_SEBTE Unreviewed; 494 AA.
AC D1ALR9;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN OrderedLocusNames=Sterm_0303 {ECO:0000313|EMBL:ACZ07187.1};
OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Sebaldella.
OX NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ07187.1, ECO:0000313|Proteomes:UP000000845};
RN [1] {ECO:0000313|Proteomes:UP000000845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA Woyke T., Wu D., Eisen J.A.;
RT "The complete chromosome of Sebaldella termitidis ATCC 33386.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ07187.1, ECO:0000313|Proteomes:UP000000845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RX PubMed=21304705;
RA Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Beck B.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Chen F.;
RT "Complete genome sequence of Sebaldella termitidis type strain (NCTC
RT 11300).";
RL Stand. Genomic Sci. 2:220-227(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000256|ARBA:ARBA00000677,
CC ECO:0000256|RuleBase:RU362042};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CP001739; ACZ07187.1; -; Genomic_DNA.
DR RefSeq; WP_012859786.1; NC_013517.1.
DR AlphaFoldDB; D1ALR9; -.
DR STRING; 526218.Sterm_0303; -.
DR KEGG; str:Sterm_0303; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_539460_0_0_0; -.
DR Proteomes; UP000000845; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 2.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 2.
DR PROSITE; PS00760; SPASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000000845};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 54..71
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 158..261
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 431..484
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 187
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 230
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 494 AA; 56646 MW; DF00A175E3AA2C8B CRC64;
MNLVLWGVFY VILTGILLYF FIKEKVIVEW LKEKEKNIAD RLASKGDLGK MKKTADIITV
VHIIILALLF WKIMDSGQDL DFSFKRNIIM VVFALNAGVL ILRKKQEWAF VVNALLLVLG
RLMMDMQGIY LYSYLALGCV LFLVEIYLYQ SQIFEAVHLI ETSITAVVIV LLIQNFYLGN
FMIPTGSMRP TIIENDRFFA NMISYKFQDP KRGDIIAFKE PKDNKLLYTK RLVGLPGETL
SIDDNGELVI NDNVIEMKAH LIGQGKKALT VTNEGLVVIL QNGYDNRTGT VYDEVINFKT
NLEGKEGTPI QVDKKGILFS DGEMLDTRVF YRKEGFLGFA GKIYIPKKDD VVKLGKIYKM
IIEQEISTQS YVINYVEVPL EEIMEQVKAG EKFTDIFYNT DNFRTTGETY IYTLNVKGKD
DTVMNILDFK YNKDTMNSLL AGQEITLTHD YYFAMGDNSS DSDDSRYWGY VQDSRIKGKL
LFRFLPITKF GIVK
//
