ID A0A0R2QYZ1_9FLAO Unreviewed; 370 AA.
AC A0A0R2QYZ1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=ABR79_06550 {ECO:0000313|EMBL:KRO54075.1};
OS Cryomorphaceae bacterium BACL11 MAG-121001-bin54.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655587 {ECO:0000313|EMBL:KRO54075.1, ECO:0000313|Proteomes:UP000051874};
RN [1] {ECO:0000313|EMBL:KRO54075.1, ECO:0000313|Proteomes:UP000051874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL11 MAG-121001-bin54 {ECO:0000313|EMBL:KRO54075.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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|ARBA:ARBA00000677,
CC 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:KRO54075.1}.
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; LIBL01000300; KRO54075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2QYZ1; -.
DR Proteomes; UP000051874; 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; 2.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 2.
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; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 2.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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 24..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 23..166
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 266..348
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 52
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 140
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 370 AA; 42734 MW; 1C9D46B55F4B31F4 CRC64;
MSWQFWKKKE NSPEKKKKSE GESWFNAILF AVIAATILRT FLIEAYTIPT SSMEKSMLVG
DFLFVSKLSY GPRVPMTPLA FPLVHHTMPI GGGKSYSESI QLPYHRMKGL GKIERNDCVV
FNWPAENIGR PVDKKENYVK RCVGIPGDVL ELKNADLFVN GAPQKEFEGM KKQWVYDVST
TGTGLNPNIL LEKYDITEGG YGRNRNEYIL TLTDANRDAI STFPNVTKVE RNVKELGVYE
DYIFPHDENH KWNVDNFGPI TIPEAGSTVE LSTENISIYK EIIERYENNK LEIIEDRIYI
NNKVATTYTF KMNYYWMMGD NRHNSADSRF WGFVPENHIV GKALFVWMSW DKNAKGLKKV
RWNRLFTSVK
//
