ID   NP30_STAAU              Reviewed;          35 AA.
AC   P21222;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   02-JUN-2021, entry version 43.
DE   RecName: Full=30 kDa neutral phosphatase;
DE            Short=NPTase;
DE            EC=3.1.-.-;
DE   Flags: Fragment;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 25923 / DSM 1104 / JCM 2413 / NBRC 14462 / NCIMB 12702 / NCTC
RC   12981 / Seattle 1945;
RX   PubMed=7888157;
RA   Yousif Y., Schiltz E., Okada K., Batsford S., Vogt A.;
RT   "Staphylococcal neutral phosphatase. A highly cationic molecule with
RT   binding properties for immunoglobulin.";
RL   APMIS 102:891-900(1994).
CC   -!- FUNCTION: Highly cationic enzyme that can bind human or rat
CC       immunoglobulins as well as serum albumin, and could therefore be
CC       involved in post-infectious sequelae.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.2-7.5. Poorly active at pH higher than 10 or lower
CC         than 5.;
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DR   PIR; S58708; S58708.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   CHAIN           1..>35
FT                   /note="30 kDa neutral phosphatase"
FT                   /id="PRO_0000057935"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         35
SQ   SEQUENCE   35 AA;  3771 MW;  9A3F432E4C2A1690 CRC64;
     KSSAEVQQTQ QASIPASQKA NLGNQNNIMX VAXYQ