ID I3YRX5_AEQSU Unreviewed; 521 AA.
AC I3YRX5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN OrderedLocusNames=Aeqsu_0220 {ECO:0000313|EMBL:AFL79743.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL79743.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL79743.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-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|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}.
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DR EMBL; CP003280; AFL79743.1; -; Genomic_DNA.
DR RefSeq; WP_014781001.1; NC_018013.1.
DR AlphaFoldDB; I3YRX5; -.
DR STRING; 746697.Aeqsu_0220; -.
DR KEGG; asl:Aeqsu_0220; -.
DR PATRIC; fig|746697.3.peg.226; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_0_10; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000006049; Chromosome.
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; IPR043739; DUF5684.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
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; PF18936; DUF5684; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 85..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 495..512
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 124..279
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 430..468
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 253
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 521 AA; 60495 MW; 6D63ECC8A20E3325 CRC64;
MSWTGWFLFF LIVQVIHFAG TWRLYQIAGR KAWEAAVPVY NAVILMKIIN RPWWWTILLF
VPIVNLIMFP VLWVETLRSF GRNSTTDTVL GILTLGLYIY YINYTKKVTH IKDRSLKPRT
STGEWVSSIL FAVVAATIVH TYVMQPFTIP TSSLEKTLLV GDFLFVSKFH YGARAPMTPI
AFPMVHDTIP VVHSKSYLTE PQIPYFRLPG FQDIKHNDIV VFNWPVDTVN AFQQYGDGKY
YYKPIDKKSN YVKRCVALPG DSLEVRDGYV FINGKKNDLP DRARIQFSYE VKVNGQLNPE
MLHNRYNITD RYGYDSNSSA YRFAAISEES LNLLKNNPNV VEITRMRGEK GQWDQSIFPN
NHNYTWNNDF FGPLYIPKKG ATVSITPETL PLYKRVIEVY EGSELGIDNK ITQSGTEVLL
NGKALTNYTF KMDYYWMMGD NRNNSEDART WGFVPFNHVV GKPVFVWMSW DGINKKVRWE
RLFTTVGGSG KPVSYLMYFV ILVIGWFAYD FWRKRKKGVK K
//
