ID A0A037ZPQ5_9RHOB Unreviewed; 449 AA.
AC A0A037ZPQ5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:KAJ57518.1};
GN ORFNames=ACMU_03150 {ECO:0000313|EMBL:KAJ57518.1};
OS Actibacterium mucosum KCTC 23349.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1454373 {ECO:0000313|EMBL:KAJ57518.1, ECO:0000313|Proteomes:UP000026249};
RN [1] {ECO:0000313|EMBL:KAJ57518.1, ECO:0000313|Proteomes:UP000026249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 23349 {ECO:0000313|EMBL:KAJ57518.1,
RC ECO:0000313|Proteomes:UP000026249};
RA Arahal D.R., Shao Z., Lai Q., Pujalte M.J.;
RT "Draft Genome Sequence of Actibacterium mucosum KCTC 23349, a Marine
RT Alphaproteobacterium with Complex Ionic Requirements Isolated from
RT Mediterranean Seawater at Malvarrosa Beach, Valencia, Spain.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:KAJ57518.1}.
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DR EMBL; JFKE01000001; KAJ57518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A037ZPQ5; -.
DR STRING; 1454373.ACMU_03150; -.
DR MEROPS; M16.019; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000026249; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 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:KAJ57518.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000026249};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..449
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001559597"
FT DOMAIN 37..182
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 191..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 449 AA; 49726 MW; 9C142A19FB1D9DCA CRC64;
MPRLFHRLLL VLLFGVAAGT ASAADVSSFK LDNGMDVVVI EDHRAPVVVN MVWYRVGAAD
EPPGKSGVAH YLEHLMFKGT EKYPNGLFSD IVEANGGSDN AFTSYDYTGY FQRVAADRLP
LMMEMEADRM TGLILTEVDA VTELDVVIEE RNQRTENSPQ ALFNEQRSAA QYLNHPYGIP
IIGWREEILG LTRQDALDFY ATYYAPNNAT LVVAGDVDPA EVLELAQTYF GPIAANPDLP
PRVRPQEPPQ RAERRLLFED PRIAQPYVVR TYLAPERNPG DQKEAAALVY LAELLGGAGA
TSVLGDELEF KQKTALYTTA FYSSLSVDPS TFGLIVLPAE GTSLQEIEDA MDTVITDFLN
TGIDQRQFET VKMQLRASGI YADDNIQGLA RRYGEALTMG LGVQDVQDWP KILQDVQPSD
VMNAAKRLFD RKRAVTGWVM RADASEVSQ
//
