ID A0A1B1NGX3_9MICO Unreviewed; 256 AA.
AC A0A1B1NGX3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=SGUI_3278 {ECO:0000313|EMBL:ANS80674.1};
OS Serinicoccus hydrothermalis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=1758689 {ECO:0000313|EMBL:ANS80674.1, ECO:0000313|Proteomes:UP000092482};
RN [1] {ECO:0000313|EMBL:ANS80674.1, ECO:0000313|Proteomes:UP000092482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT9 {ECO:0000313|EMBL:ANS80674.1,
RC ECO:0000313|Proteomes:UP000092482};
RA Tang K.;
RT "Shallow-sea hydrothermal system.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014989; ANS80674.1; -; Genomic_DNA.
DR RefSeq; WP_066642302.1; NZ_CP014989.1.
DR AlphaFoldDB; A0A1B1NGX3; -.
DR STRING; 1758689.SGUI_3278; -.
DR KEGG; serj:SGUI_3278; -.
DR PATRIC; fig|1758689.4.peg.3425; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000092482; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:ANS80674.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000092482};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 43..66
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 41..233
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 71
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 256 AA; 27868 MW; 80C57EF1428CDF2C CRC64;
MSDPRRDGRA DGEHDEPGPD PRADEHGDDG RRRGGLWAAV KEIVAIAATA LVISFLIKTF
LAQAFWIPSG SMEDTLVYGD RVMVSKVQLG SLGVDRGDIV VFEDPGGWLP PVERVDRGPV
INGALRGLEF VGVAPSSQGN HLIKRVIGLP GDTVACCDEQ GRMTVNGEPL EEDYLFPSDE
PSTSDFEITV PRDRIWLMGD HRSNSRDSRA NDDGTGEQGS VPLEDVVGQA VVLIYPFDHF
DWFTVPDTFA DVPDAP
//
