ID A0A0S6UTV0_9BRAD Unreviewed; 254 AA.
AC A0A0S6UTV0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=BDOA9_0149730 {ECO:0000313|EMBL:GAJ35764.1};
OS Bradyrhizobium sp. DOA9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1126627 {ECO:0000313|EMBL:GAJ35764.1};
RN [1] {ECO:0000313|EMBL:GAJ35764.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOA9 {ECO:0000313|EMBL:GAJ35764.1};
RX PubMed=25710540; DOI=10.1371/journal.pone.0117392;
RA Okazaki S., Noisangiam R., Okubo T., Kaneko T., Oshima K., Hattori M.,
RA Teamtisong K., Songwattana P., Tittabutr P., Boonkerd N., Saeki K.,
RA Sato S., Uchiumi T., Minamisawa K., Teaumroong N.;
RT "Genome Analysis of a Novel Bradyrhizobium sp. DOA9 Carrying a Symbiotic
RT Plasmid.";
RL PLoS ONE 10:e0117392-e0117392(2015).
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}.
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DR EMBL; DF820425; GAJ35764.1; -; Genomic_DNA.
DR RefSeq; WP_025036720.1; NZ_DF820425.1.
DR AlphaFoldDB; A0A0S6UTV0; -.
DR STRING; 1126627.BDOA9_0149730; -.
DR eggNOG; COG0681; Bacteria.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000066441; 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; 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; 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; PS00760; SPASE_I_2; 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 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 15..226
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 44
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 254 AA; 28902 MW; 16FC6564507A903A CRC64;
MSVTSGTKTE SGVGETIRVV IHALLIALVI RTFLFQPFNI PSGSMKATLL VGDYLFVSKY
SYGYSHYSIP FSPPLFSGRI WGSDPSRGDI VVFRLPKDDS TDYIKRVIGL PGDRIQMRDG
LLYINDTPVE RQRMSEYVGE DPCGSEGGGI SRVKRWKETL PNGVSYETLD CADNGYMDNT
NVYTVPAGHF FMMGDNRDNS TDSRFLGQVG YVSQEHLIGR AQMIFFSIAE GEHAWMFWRW
PWSVRWNRFF KIVR
//
