ID A3TRB6_9MICO Unreviewed; 217 AA.
AC A3TRB6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 13-SEP-2023, entry version 88.
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=JNB_19618 {ECO:0000313|EMBL:EAP97712.1};
OS Janibacter sp. HTCC2649.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP97712.1, ECO:0000313|Proteomes:UP000005063};
RN [1] {ECO:0000313|EMBL:EAP97712.1, ECO:0000313|Proteomes:UP000005063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP97712.1,
RC ECO:0000313|Proteomes:UP000005063};
RX PubMed=21075932; DOI=10.1128/JB.01298-10;
RA Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA Vergin K.L., Giovannoni S.J.;
RT "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL J. Bacteriol. 193:584-585(2011).
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: 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:EAP97712.1}.
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DR EMBL; AAMN01000004; EAP97712.1; -; Genomic_DNA.
DR AlphaFoldDB; A3TRB6; -.
DR STRING; 313589.JNB_19618; -.
DR MEROPS; S26.025; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_0_1_11; -.
DR Proteomes; UP000005063; 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; cd06462; Peptidase_S24_S26; 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; 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; PF10502; Peptidase_S26; 1.
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 Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000005063}.
FT DOMAIN 5..206
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 29
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 217 AA; 23834 MW; B338DFC7D308250C CRC64;
MGFEILLAVL AVALIQTFVV KPFGVPSQSM EQTLRIGDRI IVNRTNSTVE RGDIVVFSHG
ATWQEAQLPE SPNPLVKAAR KVGDLTGIGP SNTAYTVKRV IGLPGDLVKC CDEDGRVLVN
DKPLVEPYIY QDHAFRTPEL TCDTTPRSSR CFPEIRVPTD RLLVLGDHRS QSADSVVNCR
GGTVAEGCAR FVPLNRVVGP VVFRIWPLES FGRVNNH
//
