ID A0A4R6PKE9_9GAMM Unreviewed; 926 AA.
AC A0A4R6PKE9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:TDP38276.1};
GN ORFNames=DEU29_105128 {ECO:0000313|EMBL:TDP38276.1};
OS Idiomarina aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1327752 {ECO:0000313|EMBL:TDP38276.1, ECO:0000313|Proteomes:UP000295531};
RN [1] {ECO:0000313|EMBL:TDP38276.1, ECO:0000313|Proteomes:UP000295531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=18_TX {ECO:0000313|EMBL:TDP38276.1,
RC ECO:0000313|Proteomes:UP000295531};
RA Lamendella R.;
RT "Freshwater and sediment microbial communities from various areas in North
RT America, analyzing microbe dynamics in response to fracking.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDP38276.1}.
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DR EMBL; SNXI01000005; TDP38276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R6PKE9; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000295531; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:TDP38276.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..926
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020910631"
FT DOMAIN 59..195
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 215..389
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 502..629
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 657..836
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 926 AA; 101988 MW; FB0CF516B1BBDC5D CRC64;
MKMIKTLTAV AVSAALLGGC QMTQSANATT QTEQSVNQQQ FPEVEVSYET FKLDNGLTVV
VHEDRKAPIV AVNVWYAVGS KDEKPGKTGF AHLFEHLMFN GTENYDDEYF GPFERAGATE
MNGTTNNDRT NYFQNVPTPA LDMALWMESD RMGHLLGAVT QEKLDEQRGV VQNEKRQGEA
QPYGRVWGYL AEQTFPEGHP YSWSVIGSME DLNNASLDDV HQWFKDYYGA SNAVLVLAGD
IDVETAKEKV EKYFADIAPG KPLQKLEAWV AKREGTKRAT MQDDVPAARI YRIWNTAQLG
TADHEYLSLL SDILANGKNS RLYERLVYEE QIASSVGGFQ FGRDLAGQFF ITADAKAGVD
LDRVEAIIDE ELNRLLTEGP TQEELQRTKF STTAGFVRRV EKVGGFGGKS DLLASGEVYH
GDPGFYAKEM DWLKNATVSD LQAAGKRWLT DGDFILHVQP QPGYQAGEAQ ASRDQLPDVG
DLPTLELPEL NTFTLSNGLE VYLAERHDTP TVEMRLVADA GYAADAGTHA GTASFAMSML
KEGTENYGPM ELAAKLENLG TGLNAYASLD TSTISLNSLT VNLEQSLGLM SEIILRPTFP
QAEIDRKRSN WLEDIRKEQA RPQTQALRVV PGLMFGEDHA YSQPLTGSGT VDSINALTRD
DLVDHVQTWL RPDNARLVIV GDTTEAQIKP LLEQQLADWQ APASAKPSKV LERPAAQEQA
RVFLIDKPGT PQSLIIAGQL APSGTVDNAD TIDVMNTILG GSFTSRLNMN LREDKGWSYG
ARSMWLDNLG PGLLIALAPV QTDKTQESIE EIVKEFTQYE GENPATADEL AKVKANKVAK
LPGAYETKGQ LINAVSDTLN KGKDMQYLEA YAQRVSNIDL DSVKQTADSV LRPDAMTWVI
VGDLEQIEEK VRSLNLGEVT ILDDVK
//