ID B0C7H4_ACAM1 Unreviewed; 375 AA.
AC B0C7H4;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN OrderedLocusNames=AM1_6328 {ECO:0000313|EMBL:ABW31258.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW31258.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW31258.1, ECO:0000313|Proteomes:UP000000268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000828; ABW31258.1; -; Genomic_DNA.
DR RefSeq; WP_012166435.1; NC_009925.1.
DR AlphaFoldDB; B0C7H4; -.
DR STRING; 329726.AM1_6328; -.
DR KEGG; amr:AM1_6328; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_042005_0_0_3; -.
DR Proteomes; UP000000268; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR InterPro; IPR008353; Peptidase_S1B_tx.
DR PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR PANTHER; PTHR43019:SF36; SERINE PROTEASE RV3671C; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR01774; EXFOLTOXIN.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296};
KW Protease {ECO:0000256|RuleBase:RU004296, ECO:0000313|EMBL:ABW31258.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000268};
KW Serine protease {ECO:0000256|RuleBase:RU004296};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ SEQUENCE 375 AA; 40170 MW; 5C26EEEFBB577E36 CRC64;
MTTPKLISKF ISINALLLTA GIITPAISLH PSLVQRAVAQ SAQSTATQIY QQASPAVVTI
KNGSGHGSGF IVSADGWIIT NAHVVANGPR IVTVKFNDGR QVSADVIGFA HHGVDLAALK
IYGLTNLPSI PLSPAGSTQV GDDIFVIGTP LTEDYQNTLA RGMVSRISQQ NGTLQHSANT
NPGNSGGPIL NRQGQVVGVH FSGDLQGLVY SPTGRPIGVT KSGINFAISV DRLHTFLKAM
RSGKISRVST LPKQSQKRSI PQLANRNFNA RLEKTDIQLT PQTFIDLYQF QGKAGQSVTL
TLKSDEFNPV LQLFFVDQSS PKPKYIPVAK NDDRGPADFT AQLNLSLPQD GLYYIGVTTS
DRGEQGRYQI QAKGI
//