ID A0A2A3XH12_9GAMM Unreviewed; 267 AA.
AC A0A2A3XH12;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=lepB {ECO:0000313|EMBL:PCC22777.1};
GN ORFNames=CIK78_12370 {ECO:0000313|EMBL:PCC22777.1};
OS Halomonas sp. JB37.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2024405 {ECO:0000313|EMBL:PCC22777.1, ECO:0000313|Proteomes:UP000217454};
RN [1] {ECO:0000313|EMBL:PCC22777.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB37 {ECO:0000313|EMBL:PCC22777.1};
RX PubMed=28644126;
RA Bonham K.S., Wolfe B.E., Dutton R.J.;
RT "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL Elife 6:e22144-e22144(2017).
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}; Multi-
CC pass 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: 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:PCC22777.1}.
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DR EMBL; NRGW01000001; PCC22777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3XH12; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000217454; 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; 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.
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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 61..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 60..251
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 267 AA; 30403 MW; 05ACE8CC098E67E7 CRC64;
MDFSLLLVLA VALSGVIYLL DVVLLRPKRR QRVATADANT QEGLDEPTRE KLLKEPWPVD
YARSFFPVLL IVLVVRSFIV EPFQIPSGSM RPTLEVGDFI LVNKFAYGLR LPVVNTRFIE
VDDPERGDVM VFRFPDEPSV NFIKRVVGLP GDRIRYEGKQ LYINGEPIAK ELTEEGPEAS
PEQLLLAETL GDADHFVYNN PRDPGPQMRE VEVPAGHYFM MGDNRDHSND SRYWGFVPEE
NIVGRAFAVW MHWDGGLPSF TSVRRIE
//
