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Database: UniProt
Entry: B8FBQ7_DESAL
LinkDB: B8FBQ7_DESAL
Original site: B8FBQ7_DESAL 
ID   B8FBQ7_DESAL            Unreviewed;       987 AA.
AC   B8FBQ7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Peptidase M16C associated domain protein {ECO:0000313|EMBL:ACL04810.1};
GN   OrderedLocusNames=Dalk_3120 {ECO:0000313|EMBL:ACL04810.1};
OS   Desulfatibacillum aliphaticivorans.
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfatibacillaceae; Desulfatibacillum.
OX   NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL04810.1, ECO:0000313|Proteomes:UP000000739};
RN   [1] {ECO:0000313|EMBL:ACL04810.1, ECO:0000313|Proteomes:UP000000739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK-01 {ECO:0000313|EMBL:ACL04810.1,
RC   ECO:0000313|Proteomes:UP000000739};
RX   PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA   Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA   Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT   "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT   for anaerobic alkane oxidation.";
RL   Environ. Microbiol. 14:101-113(2012).
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DR   EMBL; CP001322; ACL04810.1; -; Genomic_DNA.
DR   RefSeq; WP_015947870.1; NC_011768.1.
DR   AlphaFoldDB; B8FBQ7; -.
DR   KEGG; dal:Dalk_3120; -.
DR   eggNOG; COG1026; Bacteria.
DR   HOGENOM; CLU_009165_1_0_7; -.
DR   Proteomes; UP000000739; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR013578; Peptidase_M16C_assoc.
DR   PANTHER; PTHR43016:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   Pfam; PF08367; M16C_assoc; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SMART; SM01264; M16C_associated; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000739}.
FT   DOMAIN          470..716
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
FT   COILED          478..520
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   987 AA;  109427 MW;  C73128EB5AAC0EAC CRC64;
     MDKQDLTPAY QPGDEISGFT LKRAVPLPRL SAVFYELKHN KTGARYIHLA NKDRENTFAV
     AFKTVPQDST GVAHILEHTA LCGSRSFPVR DPFFSMIKRS MNSFMNAFTS SDWTMYPYST
     CNQKDFYNLM QVYLDAAFFP KLDELSFKQE GFRVEEDGDG LVFKGVVYNE MKGAMSSPRD
     IMGHALMEAL YPDVTYGNNS GGDPAHIVDL THADLVAFHK RHYHPSNAFF YTYGAFPLEG
     HLKMIEERVL SEFEAIDPKT DVEFQPRWDM PKEVHQSYPV APGSDTNKKG QIAVAWLTCP
     ATDSFEVLAL DLLESVLLGN SASPLRKALI ESGLGSSLAD GTGFHADSLD TMFSVGLKNA
     DDSDPDAVKK IVFDSLNELV KEGIDKTLVD AAIHQYEFQK KEVTNNPMPY GIKLLLNLCS
     PWFHHGDPVS NLKFDDDLDR LRKEAAKGGF FEGLIKKHFL ENNHQILMVL HPDEEKAADM
     EAEEKEKLEA IAKTLTQEDR ETIRAQAQAL EKLQEAAEDV SCLPTLGRGD IDDQIQTAHP
     DPDLSTDGVS AYVQPTNGIV YYSLVARTQN LPVDLLPLLP LFCHVLPKMG SKKRDYVELT
     RDMAAYTGGI GAKATARTGY NGDGKTLEMV AFASKCLDRN LDRMFDLIKE ILFERSFADH
     KRLDTLVGEY VAALESSIIP SGHQYAISLA SRGYSRAKAI EEAWHGVHQL QTAKDLAKSI
     ADDKEAGLAD LADKLEQIAQ ALFVGDSLET GLVGEAEILA KAVKTAEALQ KDLAAQGTPR
     EGVADFSFPM PEREAWTTSS QVSFVAHVFP TVRMTHPDAP ALAVIAKMLR SLFIHREIRE
     KGGAYGGYAM SNAEEGLFGF ASYRDPQLAR TIDVFARTYD FILQGDFTDQ DVTEAILQVC
     SDIDKPDAPS TLAQKAFYAK LLGLTDEARK DYKKRVAAVT RTQVMEAAKT WFRKPQDIAP
     VAAITSKSLL EKANEQLENP LKEIAIG
//
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