ID A0A2I5TI35_SERS3 Unreviewed; 322 AA.
AC A0A2I5TI35;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN ORFNames=CWC46_08870 {ECO:0000313|EMBL:AUG99902.1}, Ser39006_008875
GN {ECO:0000313|EMBL:AUH04222.1};
OS Serratia sp. (strain ATCC 39006).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=104623 {ECO:0000313|EMBL:AUH04222.1, ECO:0000313|Proteomes:UP000017700};
RN [1] {ECO:0000313|EMBL:AUH04222.1, ECO:0000313|Proteomes:UP000017700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH04222.1}, and ATCC 39006 / SC
RC 11482 {ECO:0000313|Proteomes:UP000017700};
RX PubMed=24336377; DOI=10.1128/genomeA.01039-13;
RA Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., Cossyleon D.,
RA McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., Stanton J.A.,
RA Brugger K., Brown S.D., Salmond G.P.;
RT "Draft genome sequence of Serratia sp. strain ATCC 39006, a model bacterium
RT for analysis of the biosynthesis and regulation of prodigiosin, a
RT carbapenem, and gas vesicles.";
RL Genome Announc. 1:E01039-E01039(2013).
RN [2] {ECO:0000313|EMBL:AUH04222.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH04222.1};
RA Wang G., Yang Y., Su Y.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AUG99902.1, ECO:0000313|Proteomes:UP000233778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUG99902.1,
RC ECO:0000313|Proteomes:UP000233778};
RA Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA Fineran P.C.;
RT "Complete genome sequence of Serratia sp. ATCC 39006 LacA.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AUH04222.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH04222.1};
RA Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA Fineran P.C.;
RT "Complete genome sequence of Serratia sp. ATCC 39006.";
RL Submitted (NOV-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:RU003993};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362042}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, 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}.
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DR EMBL; CP025085; AUG99902.1; -; Genomic_DNA.
DR EMBL; CP025084; AUH04222.1; -; Genomic_DNA.
DR RefSeq; WP_021016947.1; NZ_CP025085.1.
DR AlphaFoldDB; A0A2I5TI35; -.
DR STRING; 104623.Ser39006_03686; -.
DR KEGG; sera:Ser39006_008875; -.
DR KEGG; serq:CWC46_08870; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000017700; Chromosome.
DR Proteomes; UP000233778; Chromosome.
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; 1.
DR Gene3D; 2.170.230.10; -; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
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; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR019766; Sign_pep_all-beta_subdom.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003993};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Reference proteome {ECO:0000313|Proteomes:UP000017700};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 60..300
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 322 AA; 35859 MW; 116A6E620631C882 CRC64;
MANMFALILA LATLVTGVIW CFERFRWAPA RRAKVAALSH SSDGTIDQKT LSNNLKQPGW
IETCVSVFPV LALVFIVRSF ILEPFQIPSG SMMPTLLIGD FILVEKFAYG IKDPITQTTL
IETGHPKRGD IAVFKYPRDP RLDYIKRVIG LPGDRVSYDP IAKQVTVQPA CSGQQHCDKA
LAITYSDVQP SNFVQTFNST GHEVSSGFYQ IPVGESSDGI RMNTREETLG KVTHHILTLP
GAQDQLGLYY QQPHQPLGTW VVPAGHYFMM GDNRDDSADS RYWGFVPEKN LVGKATAIWM
SFEKQEGEWP TGVRLSRIGG IH
//
