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Database: UniProt
Entry: A3U5L8_CROAH
LinkDB: A3U5L8_CROAH
Original site: A3U5L8_CROAH 
ID   A3U5L8_CROAH            Unreviewed;       927 AA.
AC   A3U5L8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   SubName: Full=Metalloprotease, putative {ECO:0000313|EMBL:EAP87535.1};
GN   OrderedLocusNames=CA2559_02230 {ECO:0000313|EMBL:EAP87535.1};
OS   Croceibacter atlanticus (strain ATCC BAA-628 / HTCC2559 / KCTC 12090).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Croceibacter.
OX   NCBI_TaxID=216432 {ECO:0000313|EMBL:EAP87535.1, ECO:0000313|Proteomes:UP000002297};
RN   [1] {ECO:0000313|EMBL:EAP87535.1, ECO:0000313|Proteomes:UP000002297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-628 / HTCC2559 / KCTC 12090
RC   {ECO:0000313|Proteomes:UP000002297};
RX   PubMed=20639333; DOI=10.1128/JB.00733-10;
RA   Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT   "The complete genome sequence of Croceibacter atlanticus HTCC2559T.";
RL   J. Bacteriol. 192:4796-4797(2010).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family.
CC       {ECO:0000256|ARBA:ARBA00006006}.
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DR   EMBL; CP002046; EAP87535.1; -; Genomic_DNA.
DR   RefSeq; WP_013186213.1; NC_014230.1.
DR   AlphaFoldDB; A3U5L8; -.
DR   STRING; 216432.CA2559_02230; -.
DR   KEGG; cat:CA2559_02230; -.
DR   eggNOG; COG3291; Bacteria.
DR   HOGENOM; CLU_007507_0_0_10; -.
DR   OrthoDB; 5377264at2; -.
DR   Proteomes; UP000002297; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09596; M36; 1.
DR   CDD; cd04818; PA_subtilisin_1; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   NCBIfam; NF038113; T9SSA_dep_M36; 1.
DR   PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF02128; Peptidase_M36; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EAP87535.1};
KW   Metalloprotease {ECO:0000313|EMBL:EAP87535.1};
KW   Protease {ECO:0000313|EMBL:EAP87535.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002297};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..927
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002658990"
FT   DOMAIN          67..94
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          509..586
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          854..926
FT                   /note="Secretion system C-terminal sorting"
FT                   /evidence="ECO:0000259|Pfam:PF18962"
SQ   SEQUENCE   927 AA;  99915 MW;  1522D67BADDBAB5F CRC64;
     MKKNYSTQLL TCLLCFVFTL SGIAQDTNSI ISTYISAHKK DLKLSGAITF HTNSIGNLSN
     KNYNVAYLQQ TFNGIKVSNA NATVVLKDNK VISFKHTFIN NLETKLTGAA TAPSLTPNQA
     GTAALSALGL TDLNHVQLLD FATKEDINAL QLSQETLTAP LFYEKAANGN YVLTYEIIVK
     EPTPHWWLSK INVTTGELVS KYDLNISCNF NAPVVTDANP ALNTHTTHKH VLNTNAPSVL
     SKKSTTHSNS YTNIQSDGAI YNAFPLRVET PIHGDRELLI NPSLIATQPV DRPIPSPSGW
     HDLDGVLQTN TNGNNVAAYE DSDNSNSASS AGSLVDGGAT LLFDFPLDLT QEPDVYQDAT
     IVNLFVWNNY VHDVFYAYGF DEDNGNFQEE DYDRFTGFDI PLVTAHNGDG VAAEAQDGSG
     LNNANFATPA DGGNPRMQMF LWGASPFGEF LNVYFSGDFD GLYASTRFPF VDIPRAEDPE
     VSGSLVVIED DGAAYTGANG GTAGASPDTD DGCTSIVNAA ALNGNIAVIR RGVCTFTTKI
     YNAEDAGAIG VIIVNNVEGE GPANGGGEAT EPITIPTISI SFEDGDPMIN ALNNGESITG
     RIIDNGPLAD LVMKDGDLDQ GIIAHEYGHG ISTRLVGGRN NSNCLLSLAF EEQMGEGWSD
     FFALVMTQKL TDTAEQPRGI GTYVLGQDVL GSGIRPARYS TDFSVNDYTY EDLGNAEITV
     PHGIGFIWST IIWDMYWAFI DEYGFDADMY YGTGGNNMAL QLVMDGLKLQ TCGNVGFVDG
     RDAILMADEA LYDGANECLI RSVFARRGVG ALAFQGTAIS RMDQVPDFTI SDPLGTDCEA
     VLASQDLNKT LFTVYPNPAS HQIHINSNKN SGLANVEVYD VNGRKVISKN IDLVNTATLN
     TAKLETGIYV LQINTDNATY TQKVIIQ
//
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