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Entry: A0A1B8P0M2_HALEL
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ID   A0A1B8P0M2_HALEL        Unreviewed;       268 AA.
AC   A0A1B8P0M2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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:OBX35817.1};
GN   ORFNames=A8U91_00151 {ECO:0000313|EMBL:OBX35817.1}, DKQ62_09130
GN   {ECO:0000313|EMBL:RAW07431.1};
OS   Halomonas elongata.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=2746 {ECO:0000313|EMBL:OBX35817.1, ECO:0000313|Proteomes:UP000092504};
RN   [1] {ECO:0000313|EMBL:OBX35817.1, ECO:0000313|Proteomes:UP000092504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HEK1 {ECO:0000313|EMBL:OBX35817.1,
RC   ECO:0000313|Proteomes:UP000092504};
RA   Gaba S., Singh R.N., Abrol S., Kaushik R., Saxena A.K.;
RT   "Genome sequence of halotolerant plant growth promoting strain of Halomonas
RT   elongata HEK1 isolated from salterns of Rann of Kutch, Gujarat, India.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RAW07431.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MH25661 {ECO:0000313|EMBL:RAW07431.1};
RA   Mamani I.J., Pacheco K.B., Quispe-Ricalde M.A.;
RT   "Draft genome sequence of Halomonas elongata strain MH25661 isolated of
RT   saline creek in the Andes from Peru.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000251811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MH25661 {ECO:0000313|Proteomes:UP000251811};
RX   PubMed=30637380; DOI=10.1128/mra.00934-18;
RA   Mamani J.I., Pacheco K.B., Elorrieta P., Romoacca P., Castelan H.,
RA   Davila S., Sierra J.L., Quispe-Ricalde M.A.;
RT   "Draft Genome Sequence of Halomonas elongata MH25661 Isolated from a Saline
RT   Creek in the Andes of Peru.";
RL   Microbiol. Resour. Announc. 8:0-0(2019).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:OBX35817.1}.
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DR   EMBL; MAJD01000001; OBX35817.1; -; Genomic_DNA.
DR   EMBL; QJUB01000019; RAW07431.1; -; Genomic_DNA.
DR   RefSeq; WP_013332777.1; NZ_QJUB01000019.1.
DR   AlphaFoldDB; A0A1B8P0M2; -.
DR   PATRIC; fig|2746.7.peg.161; -.
DR   OMA; FKWAPAR; -.
DR   Proteomes; UP000092504; Unassembled WGS sequence.
DR   Proteomes; UP000251811; 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; 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, ECO:0000313|EMBL:OBX35817.1};
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   DOMAIN          61..252
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   268 AA;  30355 MW;  624E989E15D323B8 CRC64;
     MDFALLLVVA VAVTGLIWLL DLVWWRPARR ARLTADVEAG TTEGIDPAAR EKALKDPWPV
     DYARSFFPVL LVVLLLRSFL VEPFQIPSGS MRPTLEVGDF ILVNKFAYGL RLPVINTKVV
     ELGEPERGDV MVFRFPEDPS VNFIKRVIGL PGDHIRYEDK QLYVNGEPVP KQLLEAGPKE
     EPDELLMEEQ LGEVTHDIYN NPRDPGPQVR EIVVPEDHYF AMGDNRDHSN DSRYWGFVPE
     ANVVGKAFAV WMHWDGGLPS FTDVRGIH
//
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