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Database: UniProt
Entry: A0A0S7CYM5_9MICC
LinkDB: A0A0S7CYM5_9MICC
Original site: A0A0S7CYM5_9MICC 
ID   A0A0S7CYM5_9MICC        Unreviewed;       222 AA.
AC   A0A0S7CYM5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 32.
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=AHiyo1_08880 {ECO:0000313|EMBL:GAP57927.1};
OS   Arthrobacter sp. Hiyo1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1588020 {ECO:0000313|EMBL:GAP57927.1};
RN   [1] {ECO:0000313|EMBL:GAP57927.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hiyo1 {ECO:0000313|EMBL:GAP57927.1};
RX   PubMed=26764021; DOI=10.1186/s12864-016-2380-4;
RA   Hiraoka S., Machiyama A., Ijichi M., Inoue K., Oshima K., Hattori M.,
RA   Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Genomic and metagenomic analysis of microbes in a soil environment
RT   affected by the 2011 Great East Japan Earthquake tsunami.";
RL   BMC Genomics 17:53-53(2016).
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; DF952468; GAP57927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7CYM5; -.
DR   Proteomes; UP000063628; 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; 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}.
FT   DOMAIN          2..187
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   REGION          203..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        98
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   222 AA;  24417 MW;  63D2F1BCBBECE88A CRC64;
     MVVIAIVLSF LIKTFLFRAF FIPSESMVNT LDVDDRIFVN LLVPQPFALE RGDIVVFKDA
     QGWLPPTQKT TPGPFKWFQD GLVFVGLLPD ETNQHLVKRV IGLPGDRVSC CDSSARVSVN
     GTVLNESYIN PAQVPMAKSF DVVVPAGKIW VMGDNRNNSA DSREHQSVNG GFIDIADVEG
     KATVIAWPIN RWQILDNHSE VFRNVPSPSP QNTASPTAPA SK
//
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