ID A0A1T1CGH1_9FLAO Unreviewed; 518 AA.
AC A0A1T1CGH1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BXU11_10195 {ECO:0000313|EMBL:OOV27809.1};
OS Flavobacterium sp. LM5.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1938610 {ECO:0000313|EMBL:OOV27809.1, ECO:0000313|Proteomes:UP000189962};
RN [1] {ECO:0000313|EMBL:OOV27809.1, ECO:0000313|Proteomes:UP000189962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM5 {ECO:0000313|EMBL:OOV27809.1,
RC ECO:0000313|Proteomes:UP000189962};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-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:OOV27809.1}.
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DR EMBL; MUFX01000002; OOV27809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1CGH1; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000189962; 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 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..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 85..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 491..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 124..285
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 381..461
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 252
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 518 AA; 60205 MW; 54C2A112C6E46B85 CRC64;
MTLYSWFVFF LVIQIIHFLG TWKMYESAGR KRWIAAVPIY NAIVLMKIIG RPTWWTVLLF
IPVINLIMFP VVWVETLRSF GKRSTLDTIL VIATFGLYLY YVNYTQPLNH VTDRNLSPDH
KAADTVSSLL FAVIVATIVH TYFIQPFTIP TPSLEKSLLV GDFLFVSKMN YGARVPMTTV
AMPMVHDTIP LTKKKSYLNW PQLPYMRFPS IEDIKRNDIV VFNWPVDTVY KFRDKSGLRV
EKPIDKKSNY VKRCVGLPGD HLSIKDGLIY IDGKELILPE RAKPQYSYKL ALDGKTPIDF
ESLFKELDIT DPAGFMDNER RDTLYISALT KDAAERFKQV PGITAVTRIV SKETEKGVFP
HTKNWNQDNY GPIYIPQKGK TVDLNLETLP FYKTIIDDYE NRTLEINGTE IRIDGKVATT
YTFGQNYYWM MGDNRHNSED SRYWGFVPEN HIVGKPVFIW MSWDTNGKGI NKIRWDRVFT
TVNGEGQPQS YFKYFLIALI AFFIGEYFWK KRKAKNEI
//
