ID A0A0T5ZRP8_9BACT Unreviewed; 327 AA.
AC A0A0T5ZRP8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN ORFNames=XU11_C0025G0006 {ECO:0000313|EMBL:KRT65488.1};
OS Candidatus Dadabacteria bacterium CSP1-2.
OC Bacteria; Thermodesulfobacteriota; Candidatus Dadabacteria.
OX NCBI_TaxID=1640508 {ECO:0000313|EMBL:KRT65488.1, ECO:0000313|Proteomes:UP000051780};
RN [1] {ECO:0000313|EMBL:KRT65488.1, ECO:0000313|Proteomes:UP000051780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-2 {ECO:0000313|EMBL:KRT65488.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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}; 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:KRT65488.1}.
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DR EMBL; LDXN01000025; KRT65488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZRP8; -.
DR STRING; 1640508.XU11_C0025G0006; -.
DR PATRIC; fig|1640508.3.peg.1502; -.
DR Proteomes; UP000051780; 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, ECO:0000313|EMBL:KRT65488.1};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 103..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 101..304
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 130
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 327 AA; 37504 MW; 500FCB07F48278A9 CRC64;
MHIERIHLPI YTQTLKMFGI WSRESKIKKR AKRSVAIARS ILKSNISKIS PDVGKLITEK
ISQTEKALED GNLRDLTMET EGLEGVVEEH LSKFRKSRLR QNIESLLIAV ALALFIRTFI
VQPFKIPSGS MIPTLLVGDH LLVNKFIYGT RIPFTDKMVL PIHNINRGDV IVFTYPNYEN
DPSRDGIDYI KRVIGLPGDS IDIKGRNLNI NEEEVPLKYQ GEFHDERTGV GYDEYEEDLF
GNKHQVIYLK GKGSTEKGEY IPVTKVPEGY VFVMGDNRDN SQDSRFWGFV PVKDIVGKAF
LIHWSWDFGS EGILDKVRWH RVLSLIE
//
