ID A0A1F6A6C9_9BACT Unreviewed; 459 AA.
AC A0A1F6A6C9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ORFNames=A3D03_03090 {ECO:0000313|EMBL:OGG20270.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPHIGHO2_02_FULL_40_13.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798384 {ECO:0000313|EMBL:OGG20270.1, ECO:0000313|Proteomes:UP000177092};
RN [1] {ECO:0000313|EMBL:OGG20270.1, ECO:0000313|Proteomes:UP000177092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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: 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:OGG20270.1}.
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DR EMBL; MFJN01000051; OGG20270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6A6C9; -.
DR STRING; 1798384.A3D03_03090; -.
DR Proteomes; UP000177092; 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; 3.40.33.10; CAP; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR035940; CAP_sf.
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; 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; 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 Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 44..205
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 51
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 459 AA; 51866 MW; 57A460092FCDC593 CRC64;
MAKVSFWKKF IAPVFTLLIV IIVIASYPLY RQLLLQTGLI KQGIQIAGTG SMFPTFPKGT
SADEVINAKE IVAWPKMKVF PSGFNLFGIN FFSYGLQRGD IVEIENIKTE EITKVKYNEV
AGFVKRVIGL SGDKIELRDG YVYLNSNILD EPYTAKPRST YGGDFLPDCK VLTVPPQKIF
VMGDNRKASL DSRFDLGLID EKDIHLVIPI DQQEEYKTTL RDTKFDRTLA HKPTLDGYDF
VSLLNAKRKE KNIKPLTYSP LLTLSSGRRG RVMIDTDDFS FEATKSGITM KIAVKEAGYQ
NKLLAEISTR GYFESSELLE NFLEFPDTKK LLFSSEYQDI GINGVIGEIQ GCPLQVVAVH
FGGYVPPNYP KDVVDGWQKL LDNLNEASSF YEKFKNSDGI DQKKISELLN AIDLRRSHVQ
KVVVRMKANQ WLTDGEQKYV DEDKANSDKI QTLIESLSH
//
