ID A0A0R2TCS1_9FLAO Unreviewed; 537 AA.
AC A0A0R2TCS1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=ABR87_00700 {ECO:0000313|EMBL:KRO83259.1};
OS Cryomorphaceae bacterium BACL7 MAG-121220-bin83.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655595 {ECO:0000313|EMBL:KRO83259.1, ECO:0000313|Proteomes:UP000051535};
RN [1] {ECO:0000313|EMBL:KRO83259.1, ECO:0000313|Proteomes:UP000051535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL29 MAG-121220-bin83 {ECO:0000313|EMBL:KRO83259.1};
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: 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:KRO83259.1}.
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DR EMBL; LICF01000011; KRO83259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TCS1; -.
DR Proteomes; UP000051535; 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; 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.
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 513..530
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 124..265
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 447..482
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 151
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 238
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 537 AA; 61950 MW; 2CD8A3FDE526854F CRC64;
MLDFLLYYLI LNVYSSLITW KFFVANGRPA WSAWVPVYRT YGLMQISDRP RWWMILCYIP
VVDNVMSIIL TYELLHMHGF RENKHILLSI FTLGGYVGYL NYTAALERGD RDNAEIRRRM
PATVNHILFA VVAAGAIRVT TFEAYNIPTG SMEKTLMVGD YLFVSKVHYG LRLPMTPLSI
PLMHNLIPYT QVPSYLDWVR LPYARIPGFT KVKKGDAVVF NVPVDPDRPI DKKENYVKQC
VGTPGDTISV VQRELRLNGK TLGFGDRANP QWSYYVRTTG QGFNPAGLKR NFDINYLDNR
LINNQNLSDV IQITENEYMI TISQEMLPAF SAQPNIDTVL AMNTPGNNVF PEGTPPALAW
YNENYVAPGG MFPNPDGHED SVVFAWSRDN YGPYWLPAKG QSMELTFENV LKYGRAIRVY
EGHSLRQEQG IYYLDDQPAT HVTFGLDYYW MMGDNRHNSW DSRYWGPVPE DHIVGKPVFI
FWSMDQFKKG FLSSLRTERL FTVVHGHGKP TSFLWPFLIL VGLYYGWEAY RKRKTKK
//
