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Database: UniProt
Entry: A0A255ZDB8_9FLAO
LinkDB: A0A255ZDB8_9FLAO
Original site: A0A255ZDB8_9FLAO 
ID   A0A255ZDB8_9FLAO        Unreviewed;       524 AA.
AC   A0A255ZDB8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=CHX27_14470 {ECO:0000313|EMBL:OYQ38590.1};
OS   Flavobacterium aurantiibacter.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2023067 {ECO:0000313|EMBL:OYQ38590.1, ECO:0000313|Proteomes:UP000216035};
RN   [1] {ECO:0000313|EMBL:OYQ38590.1, ECO:0000313|Proteomes:UP000216035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH167 {ECO:0000313|EMBL:OYQ38590.1,
RC   ECO:0000313|Proteomes:UP000216035};
RA   Cai H.;
RT   "Flavobacterium cyanobacteriorum sp. nov., isolated from cyanobacterial
RT   aggregates in a eutrophic lake.";
RL   Submitted (JUL-2017) 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: 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:OYQ38590.1}.
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DR   EMBL; NOXX01000226; OYQ38590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255ZDB8; -.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000216035; 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; IPR043739; DUF5684.
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; PF18936; DUF5684; 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   Reference proteome {ECO:0000313|Proteomes:UP000216035};
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        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        500..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          125..291
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          429..469
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   524 AA;  59938 MW;  45A0F9E022FD1C2D CRC64;
     MTFSEWLIVI LIFQIIHFLG TWKLYVRAGR KAWEAAIPIY NAIVLMKIIN RPTYWVILLF
     VPVVNLIMFP VIWVETARSF GKNTLTDTWL TLLTFGFYLY VLNYAANLTY VENRSLIART
     KTGDTVSSIL FAIVVATLVH TYVMQPFQIP TSSLEKTLLV GDFLFVSKFH YGARPQMSAV
     SFPMVHDTIP VAKVKSYVYD DANKDSWKNK LQYPYVRIPG FQTIKNNDIV VFNWPCDTLF
     HMYERADRRY DKPIDKKTNY VKRCVGIAGD KLEIKQGTVY INGKAVVYPE RAKIQYVYQA
     AFDRSKPVDF NYVMKTIGST EQVGSNTKGD TIFFSALTEE GVEKLKSFSA FSGIKRRIET
     RTDSRIFGGQ LSWNADNMGP IYIPKAGTTI ALTPENLPFY KKVITEYEGP HLVKVVGNDV
     YIDNKLAKSY TFQKDYYWMM GDNRGNSLDS RYWGFVPEDH VVGKAVFVWL SLDGTASGLD
     KIRWSRMFTT VNGDGPATSY LWVFGLAVLA YFGLTRFVFK KKAA
//
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