ID W5W9J1_9PSEU Unreviewed; 542 AA.
AC W5W9J1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=KALB_3827 {ECO:0000313|EMBL:AHH97191.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH97191.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH97191.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH97191.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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; CP007155; AHH97191.1; -; Genomic_DNA.
DR RefSeq; WP_025357294.1; NZ_CP007155.1.
DR AlphaFoldDB; W5W9J1; -.
DR STRING; 1449976.KALB_3827; -.
DR KEGG; kal:KALB_3827; -.
DR PATRIC; fig|1449976.3.peg.3855; -.
DR eggNOG; COG3227; Bacteria.
DR HOGENOM; CLU_010362_0_0_11; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000019225; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 21..542
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5039759605"
FT DOMAIN 93..128
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 301..368
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 380..534
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 361
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 450
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 542 AA; 55983 MW; 198BDB7F7975330C CRC64;
MSSRRTAAIA AALAASSLIA GGIGGAATAS AQTDQLSTDG SGRVIAVEPT TPVAAPQGAS
TAGAAQSHTA RLARQFGLPV GELVLSEVRQ LPGGSIAKLQ QRIGGVPVFG AQIVQDLDGS
GALLAAVGKT SQRSEGGFPA DSTAAKAKAG KAAVDAVAKK DSTAKALRAD AAENYWYDAS
LGTDGTSATA VPAYFVPVHG ADPEDKWTVV VRAETNQVLT VWGEARHATN RVVCDAKRKI
VDLDTATLAD IRCGTGQAFG VSRAEGQAAA ATADVNKVYD YFGSAQSFYS TYTGYDLTAN
IGANYNDGRG KALRGTVRMC EISTGNDGLR HTQCPWANAF WDGEQMAFGE GVTTLDITGH
ELTHGVTQHV NGLKGGYAQA INEGMSDVFG KFIAIKANDP NATGANRWLL GVGSSIGQVR
DMKNPANSGE GPGPDRVNGK YWVGPDGDEH INAGVVGKVD YLITDGDTFN GQTVRGLGEN
KSIALWWKVE NLLRSSATFK DLGNALNTAC TTNARTGVAG TTTADCTQVA NAVKATQLLQ
NA
//
