ID A0A0Q1BS35_9FLAO Unreviewed; 525 AA.
AC A0A0Q1BS35;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=AAU57_10325 {ECO:0000313|EMBL:KQC33677.1};
OS Nonlabens sp. YIK11.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=1453349 {ECO:0000313|EMBL:KQC33677.1, ECO:0000313|Proteomes:UP000051409};
RN [1] {ECO:0000313|EMBL:KQC33677.1, ECO:0000313|Proteomes:UP000051409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIK11 {ECO:0000313|EMBL:KQC33677.1,
RC ECO:0000313|Proteomes:UP000051409};
RA Kwon Y.M., Kim S.-J.;
RT "Complete genome of flavobacterium.";
RL Submitted (APR-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: 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:KQC33677.1}.
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DR EMBL; LBMJ01000001; KQC33677.1; -; Genomic_DNA.
DR RefSeq; WP_055412838.1; NZ_LBMJ01000001.1.
DR AlphaFoldDB; A0A0Q1BS35; -.
DR STRING; 1453349.AAU57_10325; -.
DR PATRIC; fig|1453349.3.peg.2166; -.
DR Proteomes; UP000051409; 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; 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; PF18936; DUF5684; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 2.
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 53..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 500..518
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 124..288
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 434..470
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 525 AA; 60298 MW; 8ECF58A300F906AF CRC64;
MSWTGWIILF IILQIVHGAG TWKFYKAAGR QAWEAFVPVY NSVVLMKIIN RPIWWTILLF
LPVVNLIMFV VIWVETLRSF GYNKAKDTAL VVLTLGLYLY YVNYTQPLEH IKERSLKPRT
AAGEWTSSIL FAVVAATIVH TYVMQPFIIP TPSLEKTLLT GDFLFVSKFH YGPRFPMTPV
AAPMVHDTIP VLSVKSYLDR PQLPYLRLPG VSDVKRNDIV VFNWPVDTVN AFPYNDGKYH
YKPIDKKSNY VKRCVGIPGD TLSMIEGKVH INGEPLVLPE RAKLQHSFLL KTKGAQYTEE
QMNEFGITDG FQQGQLTGTN TPALSIKAAT DEAIEKLEAT GNIVEVEQTI FSDAFSQRYF
PYDGMVGNSY DNIKPFLIPA KGMTTPITYK NIDYYRRIIE VYEGSEMEIS NTINLRGNDV
YLNGKPLTEY TFLQNYYWLM GDNRHNSEDS RIWGYVPESH VVGKPVFVWM SIDWSKSLTD
MVRWDRLFTT VNGTGQPTSY FVYFVVLLII YFVVRKIMKN RKAKK
//
