ID A4GHU0_9BACT Unreviewed; 326 AA.
AC A4GHU0;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 66.
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=MBMO_EB0-39H12.0027 {ECO:0000313|EMBL:ABL97651.1};
OS uncultured marine bacterium EB0_39H12.
OC Bacteria; environmental samples.
OX NCBI_TaxID=415437 {ECO:0000313|EMBL:ABL97651.1};
RN [1] {ECO:0000313|EMBL:ABL97651.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17359257; DOI=10.1111/j.1462-2920.2006.01203.x;
RA McCarren J., Delong E.F.;
RT "Proteorhodopsin photosystem gene clusters exhibit co-evolutionary trends
RT and shared ancestry among diverse marine microbial phyla.";
RL Environ. Microbiol. 9:846-858(2007).
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}.
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DR EMBL; EF089399; ABL97651.1; -; Genomic_DNA.
DR AlphaFoldDB; A4GHU0; -.
DR MEROPS; S26.001; -.
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; IPR019757; Pept_S26A_signal_pept_1_Lys-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; PS00760; SPASE_I_2; 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..22
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 34..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 89..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 87..308
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 113
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 206
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 326 AA; 37410 MW; 55346B41D380975C CRC64;
MDTGIALALL IEIVGYLLWI RFSKSEQSRY KDIVSATMFI VALLILYRIF TLNIDFGLVL
AIASLFSAIS WAIGKFINLE ELKTESRSYF FILIIITCIR SFAYEPYQIP SRSMVPGLQI
GDFVLVNKHA YGFKFPGTNY LIGKFNPPER NDVAVFIPPH TLCEVQPTEA RPDLANLSAP
ESQLFLNRFL SLQSSRCVPM GIKYVKRIIG IPGDTVLIRG YEIWINGNKL DQREISSDSQ
QTLLEETLDE TVHIVRTLGL SEYEQYEWIV PKGRYLAIGD NRDNSLDSRA WGYFSEDYLI
GRADYIWMQW KSFSELPSLA RNQKIR
//
