ID A0A2Z6IGY8_9BURK Unreviewed; 296 AA.
AC A0A2Z6IGY8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN Name=lepB {ECO:0000313|EMBL:BBF23996.1};
GN ORFNames=SUTMEG_18870 {ECO:0000313|EMBL:BBF23996.1};
OS Sutterella megalosphaeroides.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF23996.1, ECO:0000313|Proteomes:UP000271003};
RN [1] {ECO:0000313|EMBL:BBF23996.1, ECO:0000313|Proteomes:UP000271003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF23996.1,
RC ECO:0000313|Proteomes:UP000271003};
RX PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT human faeces.";
RL Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
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}.
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DR EMBL; AP018786; BBF23996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6IGY8; -.
DR KEGG; sutt:SUTMEG_18870; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000271003; 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; 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};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Reference proteome {ECO:0000313|Proteomes:UP000271003};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 72..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 73..283
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 158
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 296 AA; 34287 MW; 82B062904CF6A781 CRC64;
MNFALILFVL TCVTFLFWVA ERWKFLPERR RKAEEAARRF EADNREAIDR GDATVIDERN
RLSERILRQP WWLEYTAGLF PVIAVVFLLR SFLFEPFRIP SGSMLPTLHI GDFILVNKFD
YGIRLPVTNT KIIPVGSPER GDVVVFKYPM DTQVDYIKRV VGLPGDTVEY RDKVLYVNGV
EQKQTGSRDF VDDSTMITLE ERDEQLGEVN HLIARDGRRP SWVPPQGILR KEKSCDYNAR
GFVCTVPEGH YFMMGDNRDN SEDSRYWGFV PDEDLVGRAV LIWANFGDMS RVGGFR
//