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Database: UniProt
Entry: R5EKE2_9GAMM
LinkDB: R5EKE2_9GAMM
Original site: R5EKE2_9GAMM 
ID   R5EKE2_9GAMM            Unreviewed;       309 AA.
AC   R5EKE2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN   ORFNames=BN779_01285 {ECO:0000313|EMBL:CCX93130.1};
OS   Succinatimonas sp. CAG:777.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Succinivibrionaceae; Succinatimonas.
OX   NCBI_TaxID=1262974 {ECO:0000313|EMBL:CCX93130.1, ECO:0000313|Proteomes:UP000018241};
RN   [1] {ECO:0000313|EMBL:CCX93130.1, ECO:0000313|Proteomes:UP000018241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:777 {ECO:0000313|Proteomes:UP000018241};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:RU003993};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Multi-
CC       pass 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}.
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:CCX93130.1}.
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DR   EMBL; CAXH010000101; CCX93130.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5EKE2; -.
DR   STRING; 1262974.BN779_01285; -.
DR   Proteomes; UP000018241; Unassembled WGS sequence.
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; 1.
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; IPR019756; Pept_S26A_signal_pept_1_Ser-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; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00501; SPASE_I_1; 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:RU003993};
KW   Membrane {ECO:0000256|RuleBase:RU003993};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018241};
KW   Transmembrane {ECO:0000256|RuleBase:RU003993};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT   TRANSMEM        63..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003993"
FT   DOMAIN          68..279
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   309 AA;  35445 MW;  652A35FADE10AF51 CRC64;
     MISLISQNLF AFVLFIATVV SGIAWGYDYK FERPKRKARL EESNANSKLS SKERKALLEP
     KNIVGQVGSL FFILLVVFLF RSFLYEPFRI PSGSMLPTLQ DGDFIAVSKW EYGIKNPLTN
     NVLFKTTEPK RGDIIVFKYP EDKNVDFIKR IVGEPGDTII YQDKHLYVLK HDAPEGSVPE
     LISTKMVESV EDEVMGFNET FDVFEESFYD GESHTIRVAP NAPIMSRYYY VQTGRPVGMW
     KVPENNYFVM GDNRDNSKDS RFWGFVPYEN IVGKTTAIWL SFDFKRKSDS ALPAWVPTAV
     RFDRIGGIK
//
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