ID F0P240_WEEVC Unreviewed; 521 AA.
AC F0P240;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=Weevi_2094 {ECO:0000313|EMBL:ADX68768.1};
OS Weeksella virosa (strain ATCC 43766 / DSM 16922 / JCM 21250 / CCUG 30538 /
OS CDC 9751 / IAM 14551 / NBRC 16016 / NCTC 11634 / CL345/78).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Weeksella.
OX NCBI_TaxID=865938 {ECO:0000313|EMBL:ADX68768.1, ECO:0000313|Proteomes:UP000008641};
RN [1] {ECO:0000313|EMBL:ADX68768.1, ECO:0000313|Proteomes:UP000008641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX PubMed=21475590;
RA Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Kopitz M., Rohde M., Goker M., Tindall B.J., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Weeksella virosa type strain (9751).";
RL Stand. Genomic Sci. 4:81-90(2011).
RN [2] {ECO:0000313|Proteomes:UP000008641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX DOI=10.4056/sigs.1603927;
RA Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Brambilla E.,
RA Kopitz M., Rohde M., Goker M., Tindall B., Detter J., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Klenk H., Kyrpides N.;
RT "Complete genome sequence of Weeksella virosa type strain (9751T).";
RL Stand. Genomic Sci. 4:81-90(2011).
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; CP002455; ADX68768.1; -; Genomic_DNA.
DR RefSeq; WP_013599156.1; NC_015144.1.
DR AlphaFoldDB; F0P240; -.
DR STRING; 865938.Weevi_2094; -.
DR KEGG; wvi:Weevi_2094; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_0_10; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000008641; 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; 2.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 2.
DR InterPro; IPR043739; DUF5684.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 2.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF18936; DUF5684; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 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:UP000008641};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 55..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 90..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 491..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 121..258
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 372..458
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 233
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 521 AA; 60990 MW; 9EEF63CC88E5FE09 CRC64;
MTIFIYWLVG FIIFNLLFGA ATFNLYKLAG KKSWEAFVPF LNIWRGLDII QRPKWWIILF
YIPIVGPIFW LILLVDLADS FGKIEIKDKV IMVLTLGLYT FYLNYVEKPK YIGPEKRKST
IVSALIFAIV LATLIHNWFV QPMIVPTGSM ENTIKIGDAL FVEKVSYGAR VPLTPFGIPY
SEFINRDMFI DKARLPYMRL PGWRDLKSND IVVFNYPTDS VYSAIDRKDA YVKRLVGMPG
DTLKISNGVL YVNGKKFIPK RDALVQHRYQ VITKAPFSDK LLYDDYGLLP HDYRLQNISN
QFVYVFEGLS DPIVSSFRKN TNVLSVEQIS RHLNDKAEYI RKDGTIDSTY TIFPVNKPWN
EDQYGPLYIP KKGDVVEINK ETLPQYINLI RKYEQNKLVV DSTNGKFEVM INDEKTNKYK
IQQDYFFMMG DNRNQSLDGR FFGYVPEDHI IGRPILIWMN ANGMFEPAPR KFLWERAFTS
INNDNPDKKS YGIYVLFALI LWLGYDFYKD RKRRKENKKF D
//
