ID A0A0W8I1H5_9MICO Unreviewed; 249 AA.
AC A0A0W8I1H5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=AVL62_09685 {ECO:0000313|EMBL:KUG51581.1};
OS Serinicoccus chungangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=767452 {ECO:0000313|EMBL:KUG51581.1, ECO:0000313|Proteomes:UP000054837};
RN [1] {ECO:0000313|EMBL:KUG51581.1, ECO:0000313|Proteomes:UP000054837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD08_5 {ECO:0000313|EMBL:KUG51581.1,
RC ECO:0000313|Proteomes:UP000054837};
RA Chander A.M., Kaur G., Nair G.R., Dhawan D.K., Kochhar R.K., Mayilraj S.,
RA Bhadada S.K.;
RT "Serinicoccus chungangenesis strain CD08_5 genome sequencing and
RT assembly.";
RL Submitted (DEC-2015) 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}.
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:KUG51581.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQBL01000032; KUG51581.1; -; Genomic_DNA.
DR RefSeq; WP_058892478.1; NZ_LQBL01000032.1.
DR AlphaFoldDB; A0A0W8I1H5; -.
DR STRING; 767452.AVL62_09685; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000054837; 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; 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};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000054837};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 36..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 34..226
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 64
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 137
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 249 AA; 26945 MW; 954D27C0AAC748E8 CRC64;
MSEPTRERGS SSHEGTPQPV ERPAPTGGFW AGLREIVMIA ATALVISFLI KTFVAQAFWI
PSGSMEETLV YGDRVMVSKV QAGPLAVDRG DVVVFEDPGG WLPPVQRVDR GPVVNAALRT
LEFVGVAPSS QGNHLIKRVI GLPGDTVECC DDEGRLVVNG EPLDEDYVFP GDEPSTTDFS
VTVPEDHIWL MGDHRSNSRD SRANDDGTGQ EGSVPLDAVV GQAVVLLYPF DHFDWFTVPD
TFADVPDTP
//
