ID R5CMF2_9BACT Unreviewed; 478 AA.
AC R5CMF2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=BN567_02735 {ECO:0000313|EMBL:CCX68963.1};
OS Prevotella sp. CAG:255.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262923 {ECO:0000313|EMBL:CCX68963.1, ECO:0000313|Proteomes:UP000017913};
RN [1] {ECO:0000313|EMBL:CCX68963.1, ECO:0000313|Proteomes:UP000017913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:255 {ECO:0000313|Proteomes:UP000017913};
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: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}.
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:CCX68963.1}.
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DR EMBL; CAWV010000089; CCX68963.1; -; Genomic_DNA.
DR RefSeq; WP_021856023.1; NZ_HF986862.1.
DR AlphaFoldDB; R5CMF2; -.
DR Proteomes; UP000017913; 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; 2.
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; 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; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 2.
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 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 65..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 69..287
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 417..453
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 99
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 251
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 478 AA; 56164 MW; 4AE52A83AAF5A133 CRC64;
MIDKEKKKLN MKVQWTKFAV VTLLYLIFLY WLESWLGLIV VPFIFDVYIT KKIRWQWWKD
SERPVRFIMS WVDALVFALV AVYFINLFFF QNYVIPSSSL EKSLLTGDYL FVSKVSYGPR
IPQTPLTMPL TQHTLPVFGC KSYIEWPQWD YRRAKGLGKV ELNDIVVFNY PAGDTLVSNP
QYQAADYYQM CYSYGSQLIM DHPDMSKLTP QQQRDWYNRV YNIGRNYILD NHPEFGSIIS
RPVDRRENYV KRCVGLPGQT LQIKDRIVYL DGKPNKEPDN VQYTYNVKLN QPLPDDLMHE
LGISMEDLTS LNQNGYMPLT KKAATALAKR RDLVASIALN TEATVGDIYP LNAYTGWTRD
NYGPVWIPQK GKTITLNMKN IAVYERPIRV YEGNQLEVKN GKIYINGKQT DKYTFKMDYY
WMMGDNRHNS ADSRYWGFVP EDHIVGKPIF IWWSSDPDRS GFSKVRWSRL FRFVDNIK
//
