ID I9N6G3_RHILT Unreviewed; 247 AA.
AC I9N6G3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=Rleg9DRAFT_2323 {ECO:0000313|EMBL:EJB03489.1};
OS Rhizobium leguminosarum bv. trifolii WSM597.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=754764 {ECO:0000313|EMBL:EJB03489.1, ECO:0000313|Proteomes:UP000005092};
RN [1] {ECO:0000313|EMBL:EJB03489.1, ECO:0000313|Proteomes:UP000005092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM597 {ECO:0000313|EMBL:EJB03489.1,
RC ECO:0000313|Proteomes:UP000005092};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R.,
RA O'Hara G., Rui T., Howieson J., Reeve W., Woyke T.;
RT "Improved High-Quality Draft Sequence of Rhizobium leguminosarum bv.
RT trifolii WSM597.";
RL Submitted (FEB-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}.
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DR EMBL; JH719381; EJB03489.1; -; Genomic_DNA.
DR RefSeq; WP_003587590.1; NZ_JH719381.1.
DR AlphaFoldDB; I9N6G3; -.
DR MEROPS; S26.001; -.
DR HOGENOM; CLU_028723_1_2_5; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000005092; 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; 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; 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|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 18..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 13..218
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 43
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 247 AA; 27940 MW; 5ED27474DD2D583A CRC64;
MSEKVEAKPN ALWENIKVII QALILAMVIR TVLFQPFTIP SGSMMPTLLV GDYIFVNKFA
YGYSKYSLPF SPDIFSGRLF GADPKRGDIV VFRFPPNPEI DYIKRCIGLP GDHIQVTDGV
LYVNGKPVPK VADGTFTSDY KLDPGADVPV FRETLDNGKT YDTLDQSPVS RGDNTREFIV
PEGHYFMMGD NRDNSLDSRF DVGFVPAENL VGRASVIFFS LGNDTSFREI WKWPTNMRWD
RLFKVVE
//
